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- W1994339526 abstract "Rabbit reticulocyte lysates and wheat germ lysates were found to contain significant neutral protease activity when assayed against the highly sensitive 7-amino-4-methylcoumarin (AMC) peptide substrates Phe-AMC, succinyl-Ala-Ala-Phe-AMC and t-boc-Ala-Ala-Pro-Ala-AMC (substrates for aminopeptidase, chymotrypsin and elastase-like enzymes, respectively). Additionally, wheat germ lysates contain a trypsin-like activity when assayed against CBZ-Gly-Gly-Arg-AMC and a post-proline cleaving activity which hydrolyzed the Pro-Ala bond of t-boc-Ala-Ala-Pro-Ala-AMC." @default.
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- W1994339526 date "1981-11-01" @default.
- W1994339526 modified "2023-09-24" @default.
- W1994339526 title "Protease activities present in wheat germ and rabbit reticulocyte lysates" @default.
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- W1994339526 doi "https://doi.org/10.1016/0006-291x(81)90489-7" @default.
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