Abstract
Congenital α 1-antitrypsin (AAT) deficiency is one of the major causes of chronic emphysema (Laurell and Eriksson, 1963; Eriksson, 1965; Gadek and Crystal, 1983). Cigarette smoking is also known to cause chronic emphysema. The abnormal degradation of the connective tissue of the lung is believed to be due to uncontrolled proteolysis by an elastolytic enzyme released from neutrophils (Mittman, 1971). This enzyme, neutrophil elastase, degrades elastin and collagen (Barrett, 1975) and, unless controlled, will ultimately cause extensive lung damage. Normally, plasma AAT (pAAT) rapidly inactivates neutrophil elastase (Beatty et al., 1980). However, when levels of pAAT are reduced, either due to congenital deficiency or by oxidative inactivation of pAAT (Johnson and Travis, 1979), enzymatic degradation of lung tissue may occur which ultimately leads to pulmonary emphysema (Travis and Salvesen, 1983). pAAT has become commercially available (Prolastin, Cutter Biological, Miles Inc., West Haven, Conn.), but the supply is limited. Development of a recombinant DNA-derived AAT (rAAT) is highly desirable. Recently, cDNA clones of AAT have been constructed in plasmids and the protein expressed by yeast cells (Rosenberg et al., 1984).
Stability and Characterization of Protein and Peptide Drugs: Case Histories, edited by Y. John Wang and Rodney Pearlman. Plenum Press, New York, 1993.
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Vemuri, S., Yu, C.T., Roosdorp, N. (1993). Formulation and Stability of Recombinant α 1-Antitrypsin. In: Wang, Y.J., Pearlman, R. (eds) Stability and Characterization of Protein and Peptide Drugs. Pharmaceutical Biotechnology, vol 5. Springer, Boston, MA. https://doi.org/10.1007/978-1-4899-1236-7_9
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DOI: https://doi.org/10.1007/978-1-4899-1236-7_9
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