Further studies of primer-independent phosphorylase isozymes in the algae |
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Authors: | Jerome F Fredrick |
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Institution: | Research Laboratories, the Dodge Chemical Company, Bronx, NY 10469, U.S.A. |
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Abstract: | Both Oscillatoria princeps and Cyanidium caldarium contain phosphorylase isozymes that can cause the synthesis of polyglucan from glucose-1-phosphate in the absence of added maltodextrin ‘primer’. In addition, O. princeps contains a primer-dependent phosphorylase isozyme. When the phosphorylase fractions isolated from extracts of the algae were treated with α-amylase, the primer-independent isozyme became primer-dependent and shifted from the position it was normally found at after polyacrylamide gel electrophoresis. This primer-independent isozyme became less mobile towards the anode, and was found at the locus usually occupied by the primer-dependent isozyme. It was not possible to restore its mobility towards the anode and its primer-independent properties by preincubation with maltoheptaose. The indication is that this isozyme is a glucoprotein and that the glucan component is chemically bonded to the protein. |
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Keywords: | Cyanophyta blue-green algae α-1 4-glucan phosphorylase primer-independent phosphorylase isozymes α-amylase action on phosphorylase glycoprotein |
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