Studies on the mung bean trypsin inhibitor--reduction and reoxidation of the disulfide bonds of the Lys active fragment.
Sci Sin B
; 27(9): 918-25, 1984 Sep.
Article
en En
| MEDLINE
| ID: mdl-6441252
ABSTRACT
Two peptide chains A1 and A2 of the Lys active fragment, linked via a couple of inter-disulfide bonds, could be separated from each other after reduction with dithiothreitol and gel filtration on Sephadex G-25. Reoxidation of the reduced peptide chain A1 resulted in recovering the inhibitory activity with 25% yield, based on the original activity of the Lys fragment. The A1 active fragment was further purified by affinity chromatography with immobilized trypsin. Sephadex G-25 gel filtration produced two forms of the A1 active fragment, the major fraction being a monomer and the minor one being a dimer with lower activity. The results obtained offered evidence of the evolution of mung bean inhibitor from an ancestral single-headed inhibitor by fused gene duplication with A2 as a connecting peptide. The CD spectra of the Lys fragment and the reoxidized peptide chain A1 were also compared.
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Banco de datos:
MEDLINE
Asunto principal:
Inhibidores de Tripsina
Idioma:
En
Revista:
Sci Sin B
Año:
1984
Tipo del documento:
Article