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β-1,3-Oligoglucan:orthophosphate glucosyltransferases fromEuglena gracilis:II. Comparative studies between laminaribiose- and β-1,3-oligoglucan phosphorylase

Authors
Journal
Biochimica et Biophysica Acta (BBA) - Enzymology
0005-2744
Publisher
Elsevier
Publication Date
Volume
146
Issue
2
Identifiers
DOI: 10.1016/0005-2744(67)90227-6
Disciplines
  • Biology

Abstract

Abstract 1. 1. Further studies have been carried out on the specificity of laminaribiose- and β-1,3-oligoglucan phosphorylase. Both enzymes, present in extracts of Euglena gracilis, could be separated either by calcium phosphate gel or by DEAE-cellulose column chromatography. 2. 2.|From the data presented it can be concluded that the two enzymes catalyze the same reaction but with different quantitative specificity. The β-1,3-oligoglucan phosphorylase was found to phosphorolyze laminaritriose and higher homologues at a greater rate than laminaribiose while the opposite behavior was observed with laminaribiose phosphorylase. 3. 3.|Another, and probably more striking, difference between the two enzymes was the fact that aged preparations of β-1,3-oligoglucan phosphorylase showed an absolute requirement of sulfhydryl donors while laminaribiose phosphorylase was only slightly activated. 4. 4.|The possibility that the qualitative similarity might be due to a cross-contamination of the enzymatic fractions was discarded by competition experiments between substrates and by the elution pattern of the DEAE-cellulose chromatography.

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