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α‐1,4‐Glucan phosphorylase forms in the green alga Eremosphaera viridis
Author(s) -
Steup Martin,
Melkonian Michael
Publication year - 1981
Publication title -
physiologia plantarum
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.351
H-Index - 146
eISSN - 1399-3054
pISSN - 0031-9317
DOI - 10.1111/j.1399-3054.1981.tb05566.x
Subject(s) - glycogen phosphorylase , molecular mass , chlorophyceae , glucan , enzyme , polyacrylamide gel electrophoresis , pigment , electrophoresis , biochemistry , biology , chemistry , chromatography , botany , algae , chlorophyta , organic chemistry
In extracts of the unicellular green alga Eremosphaera viridis DeBary (Chlorococcales, Chlorophyceae) the average specific activity of α‐1,4‐glucan phosphorylase (E.C. 2.4.1.1) was 200 nmol glucose 1‐phosphate formed per min and mg protein. Using continuous and discontinuous electrophoresis on polyacrylamide gels, three phosphorylase forms were found. When the log of the relative mobility of the three enzyme forms was plotted versus the acrylamide gel concentration (Ferguson plot) parallel lines were obtained, indicating that the three enzymes were indiscernible with respect to molecular weight. Electrophoresis on density gradient gels resulted in three activity zones lying close to each other. The relative molecular mass ( M r ) of the three enzymes was estimated to be around 180,000 with a difference of less than 7,000 between the small and the large forms.