REMOVAL OF 4 WITH SIMULTANEOUS EXCHANGE OF 6 AMINO-ACID-RESIDUES IN THE MOLECULE OF TRYPSIN-INHIBITOR III FROM SQUASH SEEDS (CMTI-III) DOESNOT AFFECT THE ASSOCIATION EQUILIBRIUM-CONSTANT WITH THE ENZYME

Authors
ROZYCKI J KUPRYSZEWSKI G ROLKA K RAGNARSSON U ZBYRYT T WILUSZ T
Citation
J. Rozycki et al., REMOVAL OF 4 WITH SIMULTANEOUS EXCHANGE OF 6 AMINO-ACID-RESIDUES IN THE MOLECULE OF TRYPSIN-INHIBITOR III FROM SQUASH SEEDS (CMTI-III) DOESNOT AFFECT THE ASSOCIATION EQUILIBRIUM-CONSTANT WITH THE ENZYME, Polish Journal of Chemistry, 69(3), 1995, pp. 367-370
Citations number
23
Categorie Soggetti
Chemistry
Journal title
Polish Journal of Chemistry → ACNP
ISSN journal
01375083
Volume
69
Issue
3
Year of publication
1995
Pages
367 - 370
Database
ISI
SICI code
0137-5083(1995)69:3<367:RO4WSE>2.0.ZU;2-O
Abstract
25-Peptide [desArg(1),des Val(2), desHis(25), desGly(29), Gly(9), Gly( 17), Pro(18), Gly(19), Gly(23), Pro(24)] CMTI-III, the proteinous tryp sin inhibitor with the shortest polypeptide chain known at present, wa s synthesized by the solid-phase method. The trypsin inhibitory activi ty of this analogue measured as association equilibrium constant (K-a) with bovine beta-trypsin is comparable with that of the wild CMTI-III inhibitor.