Journal
BIOCHIMIE
Volume 92, Issue 11, Pages 1667-1673Publisher
ELSEVIER FRANCE-EDITIONS SCIENTIFIQUES MEDICALES ELSEVIER
DOI: 10.1016/j.biochi.2010.03.021
Keywords
Chymotrypsin; Kunitz inhibitors; Plant inhibitors; Primary structure; Trypsin inhibitors
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Funding
- CAPES
- CNPq
- FAPESP
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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.
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