Please use this identifier to cite or link to this item:
Type: Artigo de periódico
Title: The Complete Amino Acid Sequence Of A Trypsin Inhibitor From Bauhinia Variegata Var. Candida Seeds
Author: Ciero L.D.
Oliva M.L.V.
Torquato R.
Kohler P.
Weder J.K.P.
Novelle J.C.
Sampaio C.A.M.
Oliveira B.
Marangoni S.
Abstract: Trypsin inhibitors of two varieties of Bauhinia variegata seeds have been isolated and characterized. Bauhinia variegata Candida trypsin inhibitor (BvcTI) and B. variegata lilac trypsin inhibitor (BvlTI) are proteins with M, of about 20,000 without free sulfhydryl groups. Amino acid analysis shows a high content of aspartic acid, glutamic acid, serine, and glycine, and a low content of histidine, tyrosine, methionine, and lysine in both inhibitors. Isoelectric focusing for both varieties detected three isoforms (pi 4.85, 5.00, and 5.15), which were resolved by HPLC procedure. The trypsin inhibitors show K, values of 6.9 and 1.2 nM for BvcTI and BvlTI, respectively. The Nterminal sequences of the three trypsin inhibitor isoforms from both varieties of Bauhinia variegata and the complete amino acid sequence of B. variegata var. Candida L. trypsin inhibitor isoform 3 (BvcTI-3) are presented. The sequences have been determined by automated Edman degradation of the reduced and carboxymethylated proteins of the peptides resulting from Staphylococcus aureus protease and trypsin digestion. BvcTI-3 is composed of 167 residues and has a calculated molecular mass of 18,529. Homology studies with other trypsin inhibitors show that BvcTI-3 belongs to the Kunitz family. The putative active site encompasses Arg (63)-Ile (64). © 1998 Plenum Publishing Corporation.
Rights: fechado
Identifier DOI: 
Date Issue: 1998
Appears in Collections:Unicamp - Artigos e Outros Documentos

Files in This Item:
There are no files associated with this item.

Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.