Isolation and characterization of rabbit plasma α-1-antiproteinase E

Biological Chemistry

Volumn 379, Issue 11, 1998, Pages 1367-1370

  Saito, Akio ^a   Sinohara, Hyogo ^b  

^a KINKI UNIVERSITY SCHOOL OF MEDICINE   (Japan)

^b KINKI UNIVERSITY   (Japan)

Author keywords

1 antitrypsin; Proteinase inhibitor; Serpin

Indexed keywords

ALPHA 1 ANTITRYPSIN; CHYMOTRYPSIN; ELASTASE; GLUTAMIC ACID; HYDROXYAPATITE; KALLIKREIN; PLASMIN; TRYPSIN;

ANION EXCHANGE CHROMATOGRAPHY; ARTICLE; COMPLEX FORMATION; ENZYME ACTIVITY; ENZYME INHIBITION; ENZYME ISOLATION; NONHUMAN; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRIORITY JOURNAL; RABBIT;

ALPHA 1-ANTITRYPSIN; ANIMALS; CHYMOTRYPSIN; ISOMERISM; PANCREATIC ELASTASE; RABBITS; SUCCINIMIDES; TRYPSIN; TRYPSIN INHIBITORS;

ORYCTOLAGUS CUNICULUS;

EID: 0031732895     PISSN: 14316730     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article

References (18)

1. Boswell, D.R., and Bathurst, I.C. (1985). Molecular physiology and pathology of α-1-antitrypsin. Biochem. Educ. 13, 98-104.
2. Carrell, R., and Travis, J. (1985). α-1-Antitrypsin and the serpins: variation and countervariation. Trends Biochem. Sci. 10, 20-24.
3. Coleman, P.L., Latham, H.G. Jr., and Shaw, E.N. (1976). Some sensitive methods for the assay of trypsinlike enzymes. Methods Enzymol. 45, 12-26.
4. Green, N.M., and Work, E. (1953). Pancreatic trypsin Inhibitor: 2. Reaction with trypsin. Biochem. J. 54, 347-352.
5. Guzdek, A., Potempa, J., Dubin, A., and Travis, J. (1990). Comparative properties of human α-1 -proteinase inhibitor glycosylation variants. FEBS Lett. 272, 125-127.
6. Heidtmann, H., and Travis, J. (1986). Human α-1-proteinase inhibitor. In: Proteinase Inhibitors, A. J. Barren and G.S. Salvesen, eds. (Amsterdam, The Netherlands: Elsevier), pp. 441-456.
7. Jallat, S., Carvallo, D., Tessier, L.H., Roecklin, D., Roitsch, C., Ogushi, F., Crystal, R.G., and Courtney, M. (1986). Altered specificities of genetically engineered α-1-antitrypsin variants. Protein Eng. 1, 29-35.
8. Johnson, D., and Travis, J. (1979). The oxidative inactivation of human α-1-proteinase inhibitor. J. Biol. Chem. 254, 4022-4026.
9. Koj, A., Hatton, M.W.C., Wong, K.-L, and Regoeczi, E. (1978). Isolation and partial characterization of rabbit plasma α-1-antitrypsin. Biochem. J. 169, 589-596.
10. Patterson, S.D. (1991). Mammalian α-1-antitrypsins: Comparative biochemistry and genetics of the major plasma serpin. Comp. Biochem. Physiol. 100B, 439-454.
11. Saito, A., and Sinohara, H. (1988). Differential interactions of rabbit plasma α-1-antiproteinases S and F with porcine trypsin. J. Biochem. 103, 247-253.
12. Salto, A., and Sinohara, H. (1990). Amino acid sequence at the reactive site of rabbit α-1-antitproteinases. J. Biochem. 108, 80-85.
13. Saito, A., and Sinohara, H. (1995). Rabbit α-1-antiproteinase E: A novel recombinant serpin which does not inhibit proteinases. Biochem. J. 307, 369-375.
14. Saito, A., and Sinohara, H. (1998). Various forms of rabbit α-1-antiproteinases. Biochem. Mol. Biol. Int., 46, 27-34.
15. Sambrook, J., Fritsch, E.F., and Maniatis, T. (1989). Molecular Cloning, a Laboratory Manual, 2nd ed. (Cold Spring Harbor, New York: Cold Spring Harbor Laboratory Press).
16. Takahara, H., and Sinohara, H. (1983). Inhibitory spectrum of mouse contrapsin and α-1-antitrypsin against mouse serine proteases. J. Biochem. 93, 1411-1419.
17. Travis, J., and Salvesen, G.S. (1983). α-1-Proteinase inhibitor. Annu. Rev. Biochem. 52, 663-674.
18. Wardell, M.R., Chang, W.-S.W., Bruce, D., Skinner, R., Lesk, A.M., and Carrell, R.W. (1997). Preparative induction and characterization of L-anthithrombin: A structural homologue of latent plasminogen activator inhibitor-1. Biochemistry 36, 13133-13142.