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Purification and partial characterisation of trypsin inhibitors from seeds of Clitoria ternatea
Author(s) -
Macedo Maria Ligia R,
XavierFilho José
Publication year - 1992
Publication title -
journal of the science of food and agriculture
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.782
H-Index - 142
eISSN - 1097-0010
pISSN - 0022-5142
DOI - 10.1002/jsfa.2740580110
Subject(s) - clitoria ternatea , trypsin , arginine , chymotrypsin , biochemistry , lysine , chemistry , biology , enzyme , amino acid , medicine , alternative medicine , pathology
Three trypsin inhibitors of 20, 12 and 7 kDa were isolated in pure form from seeds of the vine Clitoria ternatea L of the tribe Glycineae of the Papilionoideae. The 20‐kDa inhibitor is a one‐chain molecule with arginine in the reactive site. The 12‐kDa one is also a one‐chain molecule and has lysine in the reactive site. It is also an inhibitor of chymotrypsin. They were tentatively assigned to the Kunitz and Bowman‐Birk families, respectively. The small molecular weight inhibitor (7 kDa) also has an arginine in the reactive site and is probably of the Bowman‐Birk type.