Alpha 1-antitrypsin
Alpha 1-antitrypsin Uses, Dosage, Side Effects, Food Interaction and all others data.
Human alpha-1 proteinase inhibitor or alpha-1-antitrypsin, prepared from human plasma via Cohn alcohol fractionation followed by PEG and zinc chloride fractionation.
Prevents excessive accumulation of active neutrophil elastase and consequent proteolysis of elastin tissues in alveolar lung structures. This prevents the development of emphysema.
Trade Name | Alpha 1-antitrypsin |
Generic | Alpha-1-proteinase inhibitor |
Alpha-1-proteinase inhibitor Other Names | Alfa 1-proteinase inhibitor (human), Alfa-1-antitripsina, Alfa1 antitrypsin, Alpha 1-antitrypsin, Alpha 1-Proteinase Inhibitor, Alpha 1-proteinase inhibitor (human), Alpha 1-proteinase inhibitor, human, Alpha-1 protease inhibitor, Alpha-1 proteinase inhibitor (human), Alpha-1-antiproteinase, Alpha-1-antitrypsin, Alpha-1-proteinase Inhibitor (human), Alpha-1-proteinase inhibitor human, Alpha-1-proteinase Inhibitor, Human, Alpha-1-proteinase inhibitor,human, Alpha1-proteinase Inhibitor, Alpha1-proteinase inhibitor (human), alpha1-proteinase inhibitor human |
Type | |
Formula | C2001H3130N514O601S10 |
Weight | 44324.5 Da |
Groups | Approved |
Therapeutic Class | |
Manufacturer | |
Available Country | |
Last Updated: | September 19, 2023 at 7:00 am |
Uses
Alpha 1-antitrypsin is a purified form of human alpha-1 proteinase inhibitor used to treat emphysema patients with associated alpha-1 proteinase inhibitor deficiency.
For chronic augmentation and maintenance therapy in individuals with alpha1-proteinase inhibitor (A1-PI) deficiency and clinical evidence of emphysema.
Alpha 1-antitrypsin is also used to associated treatment for these conditions: Emphysema
How Alpha 1-antitrypsin works
Alpha-1 proteinase inhibitor is a serine protease inhibitor (Serpin). Its primary mechanism is inhibiting the action of the serine protease called elastase (also plasmin and thrombin) in the lungs. The reactive center loop (RCL) of alpha-1 proteinase inhibitor extends out from the body of the protein and directs binding to the target protease. The protease cleaves the serpin at the reactive site, establishing a covalent linkage between the carboxyl group of the serpin reactive site and the serine hydroxyl of the protease. The resulting inactive serpin-protease complex is highly stable.
Food Interaction
No interactions found.Volume of Distribution
- 5632 ± 2006 mL [ARALAST NP]
- 5618 ± 1618 mL [Aralast]
Clearance
- 940 +/- 275 mL/day [Patients with congenital α1-PI deficiency with single IV infusion of 60 mg/kg]
Innovators Monograph
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