| Autor: |
Levleva, E., Rudenskaya, Yu., Zimacheva, A., Mosolov, V. |
| Zdroj: |
Applied Biochemistry & Microbiology; Sep2000, Vol. 36 Issue 5, p466-468, 3p |
| Abstrakt: |
A protein that inhibited the proteolytic activity of trypsin was isolated from amaranth leaves ( Amaranthus cruentus) by affinity chromatography on trypsin-Sepharose. The inhibition was noncompetitive (with p-nitroanilide- N-α-benzoyl-DL-arginine as substrate) and had a K i, of 1.87 × 10−7 M. The protein caused a weaker inhibitory effect on chymotrypsin, had no effect on subtilisin, displayed a molecular weight of 8 kDa, and contained no cysteine residues. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
| Externí odkaz: |
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