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- W2035667068 abstract "A maize root endopeptidase which has maximum activity on N-t-butoxycarbonyl- L -alanine p-nitrophenyl ester (Boc-Ala-ONp) at pH 6.7 was inhibited by the histidine-specific reagents diethylpyrocarbonate and diethyl-p-nitrophenyl phosphate. Diisopropyl fluorophosphate also inhibited the endopeptidase indicating that it has the serine type reaction mechanism. It was not inhibited by iodoacetate or leupeptin but was inhibited by HgCl2. The high activity of the maize root enzyme on Boc-Ala-ONp and its inhibition by elastatinal suggest a similarity to elastase. The maize root endopeptidase gave a specific cleavage of the oxidized insulin B chain at the Ala14-Leu15 peptide bond. Only after prolonged treatment, or with high levels of the enzyme, did further hydrolysis of the two primary fragments of insulin occur." @default.
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- W2035667068 date "1989-02-01" @default.
- W2035667068 modified "2023-09-27" @default.
- W2035667068 title "Characteristics of the active site and substrate specificity of a maize root endopeptidase" @default.
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- W2035667068 doi "https://doi.org/10.1016/s0304-4165(89)80020-0" @default.
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