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- W2060994507 abstract "Additional properties of amylo-i,6-glucosidase have been studied using a rapid spectrophotometric assay. The ph optimum is in the region between 7.2 to 7.6. The enzyme is inhibited by p-chloromercuribenzoate and o-iodosobenzoate. The inhibition is reversed by glutathione. No inhibition has been observed with glucose but the “debranched” phosphorylase limit dextrin proved an inhibitor of the competitive type with a KI of 50.5 mg per cent. The variation of Km with pH has been determined and indicates that an ionizable enzymic group with a pKa of 7.5–7.6 is involved in combining with substrate. No evidence for significant reversibility of the reaction could be found under the conditions tested." @default.
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- W2060994507 date "1956-01-01" @default.
- W2060994507 modified "2023-10-14" @default.
- W2060994507 title "Studies on amylo-1,6-glucosidase" @default.
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- W2060994507 doi "https://doi.org/10.1016/0006-3002(56)90262-1" @default.
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