Protease activities present in wheat germ and rabbit reticulocyte lysates |
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| Authors: | R A Mumford C B Pickett M Zimmerman A W Strauss |
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| Institution: | 1. Department of Immunology, Merck Sharp & Dohme Research Laboratories, Rahway, N.J. 07065 USA;2. Department of Biochemistry, Merck Sharp & Dohme Research Laboratories, Rahway, N.J. 07065 USA;3. Department of Pediatrics Washington University School of Medicine, St. Louis, Mo. 63310 USA;4. Department of Biological Chemistry Washington University School of Medicine, St. Louis, Mo. 63310 USA |
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| 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. |
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