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Document Type

Research

Abstract

The dependence of the maximal velocity, Vm with pH for barley malt phosphatase has been studied from pH 4.0 to 5.4. The data show that an ionizable group in the enzyme-substrate complex with a pK2 of 4-4.6 is important for enzymic activity. These results suggest strongly the involvement of a carboxyl group of a glutamic or aspartic acid residue at the active site of this enzyme.

Publication Date

1965

Journal Title

Proceedings of the Iowa Academy of Science

Volume

72

Issue

1

First Page

113

Last Page

116

Copyright

© Copyright 1965 by the Iowa Academy of Science, Inc.

Language

EN

File Format

application/pdf

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