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Studies on the Structure and Function of Glucosephosphate Isomerases: Chemical Modifications, Chemical Cleavages and Structural Analyses

Human glucosephosphate isomerase was subjected to a series of chemical modifications aimed at identifying residues essential for catalytic activity. Specific lysyl, arginyl, tryptophanyl and histidyl residues were found to react stoichiometrically with pyridoxal-5'-phosphate-NaBH4, 2,3-butadione, N-bromosuccinimide and N-bromoacetylethanolamine phosphate, respectively.

Identiferoai:union.ndltd.org:unt.edu/info:ark/67531/metadc798042
Date12 1900
CreatorsLu, Hsieng Sen
PublisherNorth Texas State University
Source SetsUniversity of North Texas
LanguageEnglish
Detected LanguageEnglish
TypeThesis or Dissertation
FormatText
RightsPublic, Copyright, Copyright is held by the author, unless otherwise noted. All rights

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