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- W2026811523 abstract "In presence of substrate the inhibiting effect of thiol reagents is vastly decreasing. The enzyme molecule undergoes certain structural changes as a cause of „induced adaptation”︁, thus rendering the internal SH-groups inaccessible. Those free SH-groups on the surface play no significant role in the reaction catalyzed by the enzyme. On the Kinetics of Amylolysis. Part V. Examination of the SH-Groups of Wheat-β-Amylase — Proof of Induced Adaptation. During titration of wheat-β-amylase with p-chlorine mercury benzoate (pCMB) it was stated that the enzyme protein contains four sulfhydryl-groups (SH-groups) per molecule two of which are lying freely on the surface, whereas two are „hidden”︁. In absence of substrate thiol reagents instantly react with the SH-groups. pCMB and N-ethyl maleinimide cause an almost complete inhibition which is non-competitive in the case of pCMB as was demonstrated in reaction kinetic tests." @default.
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- W2026811523 date "1973-01-01" @default.
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- W2026811523 title "Über die Kinetik der Amylolyse. Teil V. Untersuchung der SH-Gruppen der Weizen-beta-Amylase und Nachweis der induzierten Anpassung" @default.
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- W2026811523 doi "https://doi.org/10.1002/star.19730251208" @default.
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