A novel subclassification for Kunitz proteinase inhibitors from leguminous seeds

被引：100

作者：

Oliva, Maria Luiza V. ^{[1
]}

Silva, Mariana C. C. ^{[1
]}

Sallai, Roberto C. ^{[1
]}

Brito, Marlon V. ^{[1
]}

Sampaio, Misako U. ^{[1
]}

机构：

[1] Univ Fed Sao Paulo, Dept Biochem, Escola Paulista Med, BR-04044020 Sao Paulo, Brazil

来源：

BIOCHIMIE | 2010年 / 92卷 / 11期

基金：

巴西圣保罗研究基金会;

关键词：

Chymotrypsin; Kunitz inhibitors; Plant inhibitors; Primary structure; Trypsin inhibitors; AMINO-ACID-SEQUENCE; FACTOR XA INHIBITOR; TRYPSIN-INHIBITOR; CHYMOTRYPSIN INHIBITOR; PROTEASE INHIBITORS; REACTIVE-SITE; BAUHINIA-BAUHINIOIDES; PLASMA KALLIKREIN; CRYSTAL-STRUCTURE; LEUCAENA-LEUCOCEPHALA;

D O I：

10.1016/j.biochi.2010.03.021

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Kunitz-type trypsin inhibitors from legume seeds have been characterized structurally. The presence of Cys-Cys in single or double chains shows a new pattern of proteins structurally not so closely related to STI. Therefore, briefly, with regard to cysteine content, plant Kunitz proteinase inhibitors may be classifed into four groups: no Cys-Cys at all, one, two and more than two Cys residues. Functional properties and diversity of these proteins are also briefly discussed. (C) 2010 Elsevier Masson SAS. All rights reserved.

引用

页码：1667 / 1673

页数：7

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