Isolation and partial amino acid sequence of the trypsin inhibitor from the seeds of Cucurbita maxima
Trypsin inhibitor from squash (Cucurbita maxima) seed was extracted with 0.1 M-acetate buffer, pH 4.5, purified on immobilized trypsin, and separated by SE-Sephadex C-50 chromatography into three active fractions. All of them inhibited trypsin to the same extent, showed no antichymotrypsin or antika...
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Published in | Acta biochimica polonica Vol. 27; no. 3/4; pp. 371 - 382 |
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Main Authors | , , , , , |
Format | Journal Article |
Language | English |
Published |
Poland
1980
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Subjects | |
Online Access | Get full text |
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Summary: | Trypsin inhibitor from squash (Cucurbita maxima) seed was extracted with 0.1 M-acetate buffer, pH 4.5, purified on immobilized trypsin, and separated by SE-Sephadex C-50 chromatography into three active fractions. All of them inhibited trypsin to the same extent, showed no antichymotrypsin or antikallikrein activity, had a similar molecular weight (about 3300), and contained no tryptophan, phenylalanine or threonine. The partial amino acid sequence of tryptic and peptic peptides of fraction III was determined by Edman degradation procedure. |
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Bibliography: | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
ISSN: | 0001-527X |