Location of the protease-inhibitory region of secretory leukocyte protease inhibitor.

作者: S P Eisenberg , K K Hale , P Heimdal , R C Thompson

DOI: 10.1016/S0021-9258(19)39026-X

关键词:

摘要: Secretory leukocyte protease inhibitor (SLPI) is a two-domain protein that inhibits wide range of proteases including chymotrypsin, elastase, and trypsin. Based on its homology to other inhibitors x-ray crystallography an SLPI-chymotrypsin complex it has been proposed the elastase chymotrypsin-inhibitory site in COOH-terminal domain trypsin-inhibitory NH2-terminal domain. We have prepared muteins SLPI by site-directed mutagenesis synthetic gene for protein, followed expression Escherichia coli. The protease-inhibitory activities these indicate leucine 72 at inhibitory chymotrypsin. Unexpectedly, our measurements not Instead they suggest also trypsin, even though amino acid residues sites trypsin are almost always either lysine or arginine.

参考文章(30)
R. Bruce Wallace, C. Garrett Miyada, [47] Oligonucleotide probes for the screening of recombinant DNA libraries Methods in Enzymology. ,vol. 152, pp. 432- 442 ,(1987) , 10.1016/0076-6879(87)52050-X
Ursula Seemüller, Marianne Arnhold, Hans Fritz, Karin Wiedenmann, Werner Machleidt, Regina Heinzel, Heribert Appelhans, Hans-Günter Gassen, Friedrich Lottspeich, The acid-stable proteinase inhibitor of human mucous secretions (HUSI-I, antileukoprotease): Complete amino acid sequence as revealed by protein and cDNA sequencing and structural homology to whey proteins and Red Sea turtle proteinase inhibitor FEBS Letters. ,vol. 199, pp. 43- 48 ,(1986) , 10.1016/0014-5793(86)81220-0
J Travis, M Owen, P George, R Carrell, S Rosenberg, R A Hallewell, P J Barr, Isolation and properties of recombinant DNA produced variants of human alpha 1-proteinase inhibitor. Journal of Biological Chemistry. ,vol. 260, pp. 4384- 4389 ,(1985) , 10.1016/S0021-9258(18)89276-6
Jurgen BECKMANN, Armin MEHLICH, Werner SCHRODER, Herbert R. WENZEL, Harald TSCHESCHE, Preparation of chemically mutated aprotinin homologues by semisynthesis: P1 substitutions change inhibitory specificity FEBS Journal. ,vol. 176, pp. 675- 682 ,(1988) , 10.1111/J.1432-1033.1988.TB14330.X
R.M. Hewick, M.W. Hunkapiller, L.E. Hood, W.J. Dreyer, A gas-liquid solid phase peptide and protein sequenator. Journal of Biological Chemistry. ,vol. 256, pp. 7990- 7997 ,(1981) , 10.1016/S0021-9258(18)43377-7
G. L. Stetler, C. Forsyth, T. Gleason, J. Wilson, R. C. Thompson, Secretion of Active, Full– and Half–Length Human Secretory Leukocyte Protease Inhibitor by Sacchammyces Cerevisiae Nature Biotechnology. ,vol. 7, pp. 55- 60 ,(1989) , 10.1038/NBT0189-55
Beatrice Kassell, Milla Radicevic, Michael J. Ansfield, M. Laskowski, THE BASIC TRYPSIN INHIBITOR OF BOVINE PANCREAS. IV. THE LINEAR SEQUENCE OF THE 58 AMINO ACIDS. Biochemical and Biophysical Research Communications. ,vol. 18, pp. 255- 258 ,(1965) , 10.1016/0006-291X(65)90749-7