Alpha₁-Proteinase Inhibitor (Human), Prolastin is a sterile, stable, lyophilized preparation of purified human Alpha₁-Proteinase Inhibitor (alpha₁-PI), also known as alpha₁-antitrypsin. Prolastin is intended for use in therapy of congenital alpha₁-antitrypsin deficiency.

Prolastin is prepared from pooled human plasma of normal donors by modification and refinements of the cold ethanol method of Cohn.¹ Part of the fractionation may be performed by another licensed manufacturer. In order to reduce the potential risk of transmission of infectious agents, Prolastin has been heat-treated in solution at 60±0.5°C for not less than 10 hours. However, no procedure has been found to be totally effective in removing viral infectivity from plasma fractionation products. In vitro studies designed to evaluate the capacity of the Prolastin manufacturing process to remove/inactivate viruses have been conducted to provide additional assurance of the viral safety profile as shown in the table below.

Process Step	Log10 Virus Reduction
	HIV-1*	BVDV**	PRV***	Reo†	HAV† †	PPV‡
Fractionation of Effluent I to II+III	3.4	3.5	3.9	2.1	1.4	1.0
PEG Precipitation	4.4	3.2	3.4	3.4	3.1	3.3
Depth Filtration	≥ 4.7	4.1	≥ 4.7	≥ 4.0	≥ 2.8	≥ 4.3
Pasteurization	≥ 6.3	4.8	≥ 4.8	N/A	N/A	N/A
Accumulated Log10 Reduction	≥ 18.8	15.6	≥ 16.8	≥ 9.5	≥ 7.3	≥ 8.6
*Human immunodeficiency virus, type 1 **Bovine viral diarrhea virus (BVDV) was chosen to model hepatitis C virus ***Pseudorabies virus (PRV) was used as a surrogate for hepatitis B virus and the human herpes viruses † Reovirus type 3 (Reo) was chosen to model non-enveloped viruses † † Human hepatitis A virus (HAV). ‡Porcine parvovirus (PPV) was selected as a surrogate for human parvovirus B19

The specific activity of Prolastin is ≥ 0.35 mg functional alpha₁-PI/mg protein and when reconstituted as directed, the concentration of alpha₁-PI is ≥ 20 mg/mL. When reconstituted, Prolastin has a pH of 6.6–7.4, a sodium content of 100–210 mEq/L, a chloride content of 60–180 mEq/L, a sodium phosphate content of 0.015–0.025 M, a polyethylene glycol content of not more than (NMT) 5 ppm, and NMT 0.1% sucrose. Prolastin contains small amounts of other plasma proteins including alpha2-plasmin inhibitor, alpha₁- antichymotrypsin, C₁-esterase inhibitor, haptoglobin, antithrombinIII, alpha₁-lipoprotein, albumin, and IgA.¹ Each vial of Prolastin contains the labeled amount of functionally active alpha₁-PI in milligrams per vial (mg/vial), as determined by capacity to neutralize porcine pancreatic elastase.¹ Prolastin contains no preservative and must be administered by the intravenous route.

REFERENCES

1.Coan MH, Brockway WJ, Eguizabal H, et al: Preparation and properties of alpha₁-proteinase inhibitor concentrate from human plasma. Vox Sang 48(6):333-42, 1985.

Last updated on RxList: 10/6/2008

Congenital Alpha₁-Antitrypsin Deficiency

Alpha₁-Proteinase Inhibitor (Human), Prolastin is indicated for chronic replacement therapy of individuals having congenital deficiency of alpha₁-PI (alpha₁-antitrypsin deficiency) with clinically demonstrable panacinar emphysema. Clinical and biochemical studies have demonstrated that with such therapy, it is possible to increase plasma levels of alpha₁-PI, and that levels of functionally active alpha₁-PI in the lung epithelial lining fluid are increased proportionately._18-20 As some individuals with alpha₁-antitrypsin deficiency will not go on to develop panacinar emphysema, only those with evidence of such disease should be considered for chronic replacement therapy with Prolastin.²² Subjects with the PiMZ or PiMS phenotypes of alpha₁-antitrypsin deficiency should not be considered for such treatment as they appear to be at small risk for panacinar emphysema.²² Clinical data are not available as to the long-term effects derived from chronic replacement therapy of individuals with alpha₁-antitrypsin deficiency with Prolastin. Only adult subjects have received Prolastin to date.

Prolastin is not indicated for use in patients other than those with PiZZ, PiZ(null) or Pi(null)(null) phenotypes.

FOR INTRAVENOUS USE ONLY

Each bottle of Alpha1-Proteinase Inhibitor (Human), Prolastin has the functional activity, as determined by inhibition of porcine pancreatic elastase,¹ stated on the label of the bottle.

The “threshold” level of alpha₁-PI in the serum believed to provide adequate anti-elastase activity in the lung of individuals with alpha₁-antitrypsin deficiency is 80 mg/dL (based on commercial standards for alpha₁-PI immunologic assay).^12,15,17 However, assays of alpha₁-PI based on commercial standards measure antigenic activity of alpha₁-PI, whereas the labeled potency value of alpha₁-PI is expressed as actual functional activity, i.e., actual capacity to neutralize porcine pancreatic elastase. As functional activity may be less than antigenic activity, serum levels of alpha₁-PI determined using commercial immunologic assays may not accurately reflect actual functional alpha₁-PI levels. Therefore, although it may be helpful to monitor serum levels of alpha₁-PI in individuals receiving Prolastin, using currently available commercial assays of antigenic activity, results of these assays should not be used to determine the required therapeutic dosage.

The recommended dosage of Prolastin is 60 mg/kg body weight administered once weekly. This dose is intended to increase and maintain a level of functional alpha₁-PI in the epithelial lining of the lower respiratory tract, providing adequate anti-elastase activity in the lung of individuals with alpha₁-antitrypsin deficiency.

Alpha₁-Proteinase Inhibitor (Human), Prolastin may be given at a rate of 0.08 mL/kg/min or greater and must be administered intravenously. The recommended dosage of 60 mg/kg takes approximately 30 minutes to infuse.

Parenteral drug products should be inspected visually for particulate matter and discoloration prior to administration, whenever solution and container permit.

Safety and effectiveness in pediatric patients has not been established.

Reconstitution

Vacuum Transfer

Note: Aseptic technique should be carefully followed. All needles and vial tops that will come into contact with the product to be administered via the intravenous route should not come in contact with any nonsterile surface. Any contaminated needles should be discarded by placing in a puncture-proof container and new equipment should be used.

1. After removing all items from the box, warm the sterile water (diluent) to room temperature (25°C, 77°F).
2. Remove the plastic flip tops from each vial (Fig. A). Cleanse vial tops (grey stoppers) with alcohol swab and allow surface to dry. After cleaning, do not allow anything to touch the latex (rubber) stopper.
3. Carefully remove the plastic sheath from the short end of the transfer needle. Insert the exposed needle into the diluent vial to the hub (Fig.B).
4. Carefully grip the sheath of the other end of the transfer needle and twist to remove it.
5. Invert the diluent vial and insert the attached needle into the vial of concentrate at a 45°angle (Fig. C). This will direct the stream of diluent against the wall of the concentrate vial and minimize foaming. The vacuum will draw the diluent into the concentrate vial.
6. Remove the diluent bottle and transfer needle (Fig. D).
7. Gently swirl the concentrate bottle until the powder is completely dissolved (Fig. E). The vial should then be visually inspected for particulate matter and discoloration prior to administration.
8. Clean the top of the vial of reconstituted Alpha1-Proteinase Inhibitor (Human), Prolastin again with alcohol swab and let surface dry.
9. Attach the filter needle (from the package) to sterile syringe. Withdraw the Prolastin solution into the syringe through the filter needle (Fig. F).
10. Remove the filter needle from the syringe and replace with an appropriate injection needle for administration. Discard filter needle into a puncture-proof container.
11. The contents of more than one bottle of Prolastin may be drawn into the same syringe before administration. If more than one bottle of Prolastin is used, withdraw contents from bottles using aseptic technique. Place contents into an administration container (plastic minibag or glass bottle) using a syringe. * Avoid pushing an I.V. administration set spike into the product container stopper as this has been known to force the stopper into the vial, with a resulting loss of sterility.

A number of factors beyond our control could reduce the efficacy of this product or even result in an ill effect following its use. These include improper storage and handling of the product after it leaves our hands, diagnosis, dosage, method of administration, and biological differences in individual patients. Because of these factors, it is important that this product be stored properly, that the directions be followed carefully during use, and that the risk of transmitting viruses be carefully weighed before the product is prescribed.

*For a patient of average weight (about 70 kg) the volume needed will exceed the limit of one syringe.

Alpha1-Proteinase Inhibitor (Human), Prolastin is supplied in the following single use vials with the total alpha₁-PI functional activity, in milligrams, stated on the label of each vial. A suitable volume of Sterile Water for Injection, USP, is provided.

NDC Number	Approximate alpha1-PI Functional Activity	Diluent
13533-601-30	500 mg	20 mL
13533-601-35	1000 mg	40 mL

Storage

Prolastin should be stored at temperatures not to exceed 25°C (77°F). Freezing should be avoided as breakage of the diluent bottle might occur.

REFERENCES

1.Coan MH, Brockway WJ, Eguizabal H, et al: Preparation and properties of alpha₁-proteinase inhibitor concentrate from human plasma. Vox Sang 48(6):333-42, 1985.

12. Gadek JE, Fells GA, Zimmerman RL, et al: Antielastases of the human alveolar structures: implications for the protease-antiprotease theory of emphysema. J Clin Invest 68(4):889-98, 1981.

15. Gadek JE, Crystal RG: alpha₁-antitrypsin deficiency. In: Stanbury JB, Wyngaarden JB, Frederickson DS, et al, eds.: The Metabolic Basis of Inherited Disease. 5th ed. New York, McGraw-Hill, 1983, p.1450-67.

17. Gadek JE, Klein HG, Holland PV, et al: Replacement therapy of alpha₁-antitrypsin deficiency: reversal of pro- tease-antiprotease imbalance within the alveolar structures of PiZ subjects. J Clin Invest 68(5): 1158-65, 1981.

18. Data on file.

19. Wewers MD, Casolaro MA, Sellers SE, et al: Replacement therapy for alpha₁-antitrypsin deficiency associated with emphysema. N Engl J Med 316(17): 1055-62,1987.

20. Wewers MD, Casolaro MA, Crystal RG: Comparison of alpha-1-antitrypsin levels and antineutrophil elastase capacity of blood and lung in a patient with the alpha-1-antitrypsin phenotype null-null before and during alpha-1-antitrypsin augmentation therapy. Am Rev Respir Dis 135(3):539-43, 1987.

22. Cohen AB: Unraveling the mysteries of alpha₁-antitrypsin deficiency. N Engl J Med 314(12):778-9, 1986.

Talecris Biotherapeutics, Inc., Research Triangle Park, NC 27709, USA. FDA revision date: n/a

Last updated on RxList: 10/6/2008

Therapeutic administration of Alpha1-Proteinase Inhibitor (Human), Prolastin, 60 mg/kg weekly, has been demonstrated to be well tolerated. In clinical studies, six reactions were observed with 517 infusions of Prolastin, or 1.16%. None of the reactions was severe.¹⁸ The adverse reactions reported included delayed fever (maximum temperature rise was 38.9°C, resolving spontaneously over 24 hours) occurring up to 12 hours following treatment (0.77%), light-headedness (0.19%), and dizziness (0.19%).¹⁸ Mild transient leukocytosis and dilutional anemia several hours after infusion have also been noted.¹⁸ Since market entry, occasional reports of other flu-like symptoms, allergic-like reactions, chills, dyspnea, rash, tachycardia, and, rarely, hypotension have also been received. Rare cases of transient increase in blood pressure or hypertension and chest pain have also been reported.

No information provided.

REFERENCES

18. Data on file.

Last updated on RxList: 10/6/2008

Because this product is made from human blood, it may carry a risk of transmitting infectious agents, e.g. viruses, and, theoretically, the Creutzfeldt-Jakob (CJD) agent. The risk that such products will transmit an infectious agent has been reduced by screening plasma donors for prior exposure to certain viruses, by testing for the presence of certain current virus infections, and by inactivating and/or removing certain viruses. Despite these measures, such products can still potentially transmit disease. There is also the possibility that unknown infectious agents may be present in such products. Individuals who receive infusions of blood or plasma products may develop signs and/or symptoms of some viral infections, particularly hepatitis C. ALL infections thought by a physician possibly to have been transmitted by this product should be reported by the physician or other healthcare provider to Talecris Biotherapeutics, Inc. [1-800-520-2807].

The physician should discuss the risks and benefits of this product with the patient, before prescribing or administering it to a patient.

Alpha₁-Proteinase Inhibitor (Human), Prolastin has been heat-treated in solution at 60°C for 10 hours in order to reduce the potential for transmission of infectious agents.¹ No cases of hepatitis, either hepatitis B or hepatitis C, have been recorded to date in individuals receiving Prolastin.¹⁸ However, as all individuals received prophylaxis against hepatitis B, no conclusion can be drawn at this time regarding potential transmission of hepatitis B virus.

General

1. Administer within 3 hours after reconstitution. Do not refrigerate after reconstitution.
2. Administer only by the intravenous route.
3. As with any colloid solution, there will be an increase in plasma volume following intravenous administration of Alpha1-Proteinase Inhibitor (Human), Prolastin.²³ Caution should therefore be used in patients at risk for circulatory overload.
4. Prolastin should be given alone, without mixing with other agents or diluting solutions.
5. Product administration and handling of the needles must be done with caution. Percutaneous puncture with a needle contaminated with blood can transmit infectious virus including HIV (AIDS) and hepatitis. Obtain immediate medical attention if injury occurs.

Place needles in sharps container after single use. Discard all equipment including any reconstituted Prolastin product in accordance with biohazard procedures.

Carcinogenesis, Mutagenesis, Impairment of Fertility

Long-term studies in animals to evaluate carcinogenesis, mutagenesis, or impairment of fertility have not been conducted.

Pregnancy Category C

Animal reproduction studies have not been conducted with Alpha1-Proteinase Inhibitor (Human), Prolastinw. It is also not known whether Prolastin can cause fetal harm when administered to a pregnant woman or can affect reproduction capacity. Prolastin should be given to a pregnant woman only if clearly needed.

Nursing Mothers

It is not known whether Prolastin is excreted in human milk. Because many drugs are excreted in human milk, caution should be exercised when Prolastin is administered to a nursing woman.

Pediatric Use

Safety and effectiveness in the pediatric population have not been established.

REFERENCES

18. Data on file.

23. Finlayson JS: Albumin products. Semin Thromb Hemost 6(2):85-120, 1980. 08937789 (Rev. January 2005)

Last updated on RxList: 10/6/2008

No information provided.

Individuals with selective IgA deficiencies who have known antibody against IgA (anti-IgA antibody) should not receive Alpha1-Proteinase Inhibitor (Human), Prolastin, since these patients may experience severe reactions, including anaphylaxis, to IgA which may be present.

Last updated on RxList: 10/6/2008

Alpha₁-antitrypsin deficiency is a chronic, hereditary, usually fatal, autosomal recessive disorder in which a low concentration of alpha₁-PI (alpha₁-antitrypsin) is associated with slowly progressive, severe panacinar emphysema that most often manifests itself in the third to fourth decades of life.^2-9 [Although the terms “alpha₁- Proteinase Inhibitor” and “alpha₁-antitrypsin” are used interchangeably in the scientific literature, the hereditary disorder associated with a reduction in the serum level of alpha₁-PI is conventionally referred to as “alpha₁- antitrypsin deficiency” while the deficient protein is referred to as “Alpha1-Proteinase Inhibitor”¹⁰]. The emphysema is typically worse in the lower lung zones.^4,8,9 The pathogenesis of development of emphysema in alpha₁-antitrypsin deficiency is not well understood at this time. It is believed, however, to be due to a chronic biochemical imbalance between elastase (an enzyme capable of degrading elastin tissues, released by inflammatory cells, primarily neutrophils, in the lower respiratory tract) and alpha₁-PI (the principal inhibitor of neutrophil elastase), which is deficient in alpha₁-antitrypsin disease.^11-15 As a result, it is believed that alveolar structures are unprotected from chronic exposure to elastase released from a chronic, low-level burden of neutrophils in the lower respiratory tract, resulting in progressive degradation of elastin tissues.^11-15 The eventual outcome is the development of emphysema. Neonatal hepatitis with cholestatic jaundice appears in approximately 10% of newborns with alpha₁-antitrypsin deficiency.¹⁵ In some adults, alpha₁- antitrypsin deficiency is complicated by cirrhosis.¹⁵

A large number of phenotypic variants of alpha₁-antitrypsin deficiency exists.¹⁵ The most severely affected individuals are those with the PiZZ variant, typically characterized by alpha₁-PI serum levels 35%normal.¹⁵ Epidemiologic studies of individuals with various phenotypes of alpha₁-antitrypsin deficiency have demonstrated that individuals with endogenous serum levels of alpha₁-PI 50 mg/dL (based on commercial standards) have a risk of 80% of developing emphysema over a lifetime.^3-6,8,9,16 However, individuals with endogenous alpha₁-PI levels 80 mg/dL, in general, do not manifest an increased risk for development of emphysema above the general population background risk.^5,15 From these observations, it is believed that the “threshold” level of alpha₁-PI in the serum required to provide adequate anti-elastase activity in the lung of individuals with alpha₁-antitrypsin deficiency is about 80 mg/dL (based on commercial standards for immunologic assay of alpha₁-PI).^12,15,17

In clinical studies of Alpha₁-Proteinase Inhibitor (Human), Prolastin, 23 subjects with the PiZZ variant of congenital deficiency of alpha₁-antitrypsin deficiency and documented destructive lung disease participated in a study of acute and/or chronic replacement therapy with Prolastin.¹⁸ The mean in vivo recovery of alpha₁-PI was 4.2 mg (immunologic)/dL per mg (functional)/kg body weight administered.^18,19 The half-life of alpha₁-PI in vivo was approximately 4.5 days.^18,19 Based on these observations, a program of chronic replacement therapy was developed. Nineteen of the subjects in these studies received Prolastin replacement therapy, 60 mg/kg body weight, once weekly for up to 26 weeks (average 24 weeks of therapy). With this schedule of replacement therapy, blood levels of alpha₁-PI were maintained above 80 mg/dL (based on the commercial standards for alpha₁-PI immunologic assay).^18-20 Within a few weeks of commencing this program, bronchoalveolar lavage studies demonstrated significantly increased levels of alpha₁-PI and functional antineutrophil elastase capacity in the epithelial lining fluid of the lower respiratory tract of the lung, as compared to levels prior to commencing the program of chronic replacement therapy with Alpha₁-Proteinase Inhibitor (Human), Prolastin.^18-20

All 23 individuals who participated in the investigations were immunized with Hepatitis B Vaccine and received a single dose of Hepatitis B Immune Globulin (Human) on entry into the investigation. Although no other steps were taken to prevent hepatitis, neither hepatitis B nor non-A, non-B hepatitis occurred in any of the subjects.^18,19 All subjects remained seronegative for HIV antibody. None of the subjects developed any detectable antibody to alpha₁-PI or other serum protein.

Long-term controlled clinical trials to evaluate the effect of chronic replacement therapy with Prolastin on the development of or progression of emphysema in patients with congenital alpha₁-antitrypsin deficiency have not been performed. Estimates of the sample size required of this rare disorder and the slow, progressive nature of the clinical course have been considered impediments in the ability to conduct such a trial.²¹ Studies to monitor the long-term effects will continue as part of the postapproval process.

REFERENCES

2. Laurell CB, Eriksson S: The electrophoretic alpha₁-globulin pattern of serum in alpha₁-antitrypsin deficiency. Scand J Clin Lab Invest 15:132-40, 1963.

3. Eriksson S: Pulmonary emphysema and alpha₁-antitrypsin deficiency. Acta Med Scand 175(2):197-205, 1964.

4. Eriksson S: Studies in alpha₁-antitrypsin deficiency. Acta Med Scand Suppl 432:1-85, 1965.

5. Kueppers F, Black LF: alpha₁-antitrypsin and its deficiency. Am Rev Respir Dis 110(2):176-94, 1974.

6. Morse JO: alpha₁-antitrypsin deficiency. N Engl J Med 299:1045-8; 1099-105, 1978.

7. Black LF, Kueppers F: alpha₁-antitrypsin deficiency in nonsmokers. Am Rev Respir Dis 117(3):421-8, 1978.

8. Tobin MJ, Cook PJ, Hutchison DC: alpha₁-antitrypsin deficiency: the clinical and physiological features of pulmonary emphysema in subjects homozygous for Pi type Z. A survey by the British Thoracic Association. Br J Dis Chest 77(1):14-27, 1983.

9. Larsson C: Natural history and life expectancy in severe alpha₁-antitrypsin deficiency, Pi Z. Acta Med Scand 204(5): 345-51, 1978.

10. Pannell R, Johnson D, Travis J: Isolation and properties of human plasma alpha₁-proteinase inhibitor. Biochemistry13(26):5439-45, 1974.

11. Lieberman J: Elastase, collagenase, emphysema, and alpha₁-antitrypsin deficiency. Chest 70(1):62-7, 1976.

12. Gadek JE, Fells GA, Zimmerman RL, et al: Antielastases of the human alveolar structures: implications for the protease-antiprotease theory of emphysema. J Clin Invest 68(4):889-98, 1981.

13. Beatty K, Bieth J, Travis J: Kinetics of association of serine proteinases with native and oxidized alpha-1-proteinase inhibitor and alpha-1-antichymotrypsin. J Biol Chem 255(9):3931-4, 1980.

14. Janoff A, White R, Carp H, et al: Lung injury induced by leukocytic proteases. Am J Pathol 97(1):111-36, 1979.

15. Gadek JE, Crystal RG: alpha₁-antitrypsin deficiency. In: Stanbury JB, Wyngaarden JB, Frederickson DS, et al, eds.: The Metabolic Basis of Inherited Disease. 5th ed. New York, McGraw-Hill, 1983, p.1450-67.

16. Larsson C, Dirksen H, Sundstrom G, et al: Lung function studies in asymptomatic individuals with moderately (Pi SZ) and severely (Pi Z) reduced levels of alpha₁-antitrypsin. Scand J Respir Dis 57(6):267-80, 1976.

17. Gadek JE, Klein HG, Holland PV, et al: Replacement therapy of alpha₁-antitrypsin deficiency: reversal of pro- tease-antiprotease imbalance within the alveolar structures of PiZ subjects. J Clin Invest 68(5): 1158-65, 1981.

18. Data on file.

19. Wewers MD, Casolaro MA, Sellers SE, et al: Replacement therapy for alpha₁-antitrypsin deficiency associated with emphysema. N Engl J Med 316(17): 1055-62,1987.

20. Wewers MD, Casolaro MA, Crystal RG: Comparison of alpha-1-antitrypsin levels and antineutrophil elastase capacity of blood and lung in a patient with the alpha-1-antitrypsin phenotype null-null before and during alpha-1-antitrypsin augmentation therapy. Am Rev Respir Dis 135(3):539-43, 1987.

21. Burrows B: A clinical trial of efficacy of antiproteolytic therapy: can it be done? Am Rev Respir Dis 127(2:2): S42-3, 1983.

Last updated on RxList: 10/6/2008

No information provided. Please refer to the WARNINGS and PRECAUTIONS sections.

Last updated on RxList: 10/6/2008

IMPORTANT NOTE: This is a summary and does not contain all possible information about this product. For complete information about this product or your specific health needs, ask your health care professional. Always seek the advice of your health care professional if you have any questions about this product or your medical condition. This information is not intended as individual medical advice and does not substitute for the knowledge and judgment of your health care professional. This information does not contain any assurances that this product is safe, effective, or appropriate for you.

ALPHA-1-PROTEINASE INHIBITOR - INJECTION

COMMON BRAND NAME(S): Prolastin

USES: This medication is used to treat lung problems (emphysema) that occur with a certain inherited disease (alpha-1-proteinase inhibitor deficiency). In these patients, lung damage is caused by elastase, a natural substance that the body needs to kill bacteria in the lungs. Normally, a protein (alpha-1-proteinase inhibitor) stops elastase from working when it is no longer needed. However, in people who do not make enough of this protein, elastase does not stop working and damages the lungs. This medication replaces the missing alpha-1-proteinase inhibitor and helps to prevent further lung damage.

HOW TO USE: This medication is given by vein, usually once a week or as directed by your doctor.

Follow all instructions for proper mixing and dilution with the correct IV fluids. Mix this medication with the sterile water supplied by the manufacturer. If your brand of medication is stored in the refrigerator, allow the medication vial and the vial of water for mixing to warm to room temperature before mixing. Do not shake the mixed drug. If you have questions about using this medication properly, consult your pharmacist.

Occasionally, a few small particles may remain in the vial. These particles will be removed by the filter provided with the medication.

Learn how to store and discard needles and medical supplies safely. Consult your pharmacist.

Dosage is based on your medical condition and response to treatment.

Tell your doctor if your condition worsens after several weeks.

SIDE EFFECTS: Fever (occurring up to 12 hours after receiving the medication), dizziness, headache, sore throat, cough, drowsiness, and pain at the injection site may occur. If any of these effects persist or worsen, tell your doctor or pharmacist promptly.

Remember that your doctor has prescribed this medication because he or she has judged that the benefit to you is greater than the risk of side effects.

This medicine may make you more likely to be infected with a certain virus (parvovirus B19). Tell your doctor immediately if you notice symptoms of an infection such as fever, chills, and stuffy nose followed by rash and joint pain (usually within 2 weeks).

A very serious allergic reaction to this drug is rare. However, stop receiving the drug and seek immediate medical attention if you notice any symptoms of a serious allergic reaction, including: hives, itching, swelling, chest tightness, trouble breathing, severe dizziness, feeling faint.

This is not a complete list of possible side effects. If you notice other effects not listed above, contact your doctor or pharmacist.

Contact your doctor for medical advice about side effects. The following numbers do not provide medical advice, but in the US you may report side effects to the Food and Drug Administration (FDA) at 1-800-FDA-1088. In Canada, you may call Health Canada at 1-866-234-2345.

PRECAUTIONS: Before using alpha-1-proteinase inhibitor, tell your doctor or pharmacist if you are allergic to it; or if you have any other allergies.

This medication should not be used if you have a certain medical condition. Before using this medicine, consult your doctor or pharmacist if you have: selective IgA deficiency with antibodies to IgA.

Before using this medication, tell your doctor or pharmacist your medical history, especially of: liver disease, heart problems (e.g., heart failure).

During pregnancy, this medication should be used only when clearly needed. Discuss the risks and benefits with your doctor.

It is not known whether this drug passes into breast milk. Consult your doctor before breast-feeding.

DRUG INTERACTIONS: Your doctor or pharmacist may already be aware of any possible drug interactions and may be monitoring you for them. Do not start, stop, or change the dosage of any medicine before checking with them first.

Keep a list of all your medications with you, and share the list with your doctor and pharmacist.

OVERDOSE: If overdose is suspected, contact your local poison control center or emergency room immediately. US residents can call the US National Poison Hotline at 1-800-222-1222. Canada residents can call a provincial poison control center.

NOTES: Do not share this medication with others.

Laboratory and/or medical tests (e.g., pulmonary function tests) should be performed periodically to monitor your progress or check for side effects. Consult your doctor for more details.

Since this medication is made from human blood, there is a very small risk that you may get infections from it (e.g., viral infections such as hepatitis B). All human blood used for medical purposes is tested very carefully to prevent this from happening. If you have questions, consult your doctor or pharmacist. Discuss with your doctor whether you should be vaccinated against hepatitis B.

MISSED DOSE: If you miss a dose, contact your doctor or pharmacist immediately to establish a new dosing schedule.

STORAGE: Different brands of this medication have different storage requirements. Ask your pharmacist how to store your brand. Do not freeze. After mixing this drug, do not refrigerate. Use the mixed drug within 3 hours. Do not store in the bathroom. Keep all medicines away from children and pets.

Do not flush medications down the toilet or pour them into a drain unless instructed to do so. Properly discard this product when it is expired or no longer needed. Consult your pharmacist or local waste disposal company for more details about how to safely discard your product.

MEDICAL ALERT: Your condition can cause complications in a medical emergency. For information about enrolling in MedicAlert, call 1-800-854-1166 (USA) or 1-800-668-1507 (Canada).

Information last revised July 2008 Copyright(c) 2008 First DataBank, Inc.