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Page 1
The inhibition of pepsin action.
Inouye K, Fruton JS. Inouye K, et al. Among authors: fruton js. Biochemistry. 1968 May;7(5):1611-5. doi: 10.1021/bi00845a001. Biochemistry. 1968. PMID: 4870331 No abstract available.
New synthetic substrates for pepsin.
Inouye K, Voynick IM, Delpierre GR, Fruton JS. Inouye K, et al. Among authors: fruton js. Biochemistry. 1966 Jul;5(7):2473-83. doi: 10.1021/bi00871a044. Biochemistry. 1966. PMID: 5335288 No abstract available.
Studies on the specificity of pepsin.
Inouye K, Fruton JS. Inouye K, et al. Among authors: fruton js. Biochemistry. 1967 Jun;6(6):1765-77. doi: 10.1021/bi00858a027. Biochemistry. 1967. PMID: 5340947 No abstract available.
Pepsin as an esterase.
Inouye K, Fruton JS. Inouye K, et al. Among authors: fruton js. J Am Chem Soc. 1967 Jan 4;89(1):187-8. doi: 10.1021/ja00977a062. J Am Chem Soc. 1967. PMID: 5342279 No abstract available.
Action of pepsin on cationic synthetic substrates.
Hollands TR, Voynick IM, Fruton JS. Hollands TR, et al. Among authors: fruton js. Biochemistry. 1969 Feb;8(2):575-85. doi: 10.1021/bi00830a017. Biochemistry. 1969. PMID: 4893576 No abstract available.
The side-chain specificity of pepsin.
Trout GE, Fruton JS. Trout GE, et al. Among authors: fruton js. Biochemistry. 1969 Oct;8(10):4183-90. doi: 10.1021/bi00838a041. Biochemistry. 1969. PMID: 4899585 No abstract available.
145 results