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- W2088468983 abstract "The cyanophyte, Oscillatoria princeps, and the enigmatic hot-spring alga, Cyanidium caldarium, contain two branching isoenzymes which can act on amylose and amylopectin, converting these polyglucans into highly branched phytoglycogens. The red alga, Rhodymenia pertusa contains three branching isoenzymes, only one of which is capable of the dual activity of the other algal branching isoenzymes. The other two red algal branching isoenzymes are Q enzymes and can only act on amylose, forming moderately branched amylopectins. However, when the isoenzymes of all three algae are separated on different concentrations of polyacrylamide gel via electrophoresis, the mobilities of the isoenzymes show that the Q enzymes and the branching enzymes are related and true isoenzymic molecules. They differ only in electrical charges, probably caused by the substitution of amino acid residues in their active peptides. It is possible that if these charge isomers are due merely to amino acid substitutions, the enzymes may have been originally derived from a common catalytic molecule. The study indicates the identity of the branching isoenzymes of Oscillatoria and Cyanidium, and lends further supporting evidence to the cyanophyte origin of the enigmatic alga." @default.
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- W2088468983 date "1971-02-01" @default.
- W2088468983 modified "2023-09-26" @default.
- W2088468983 title "Polyglucan Branching Isoenzymes of Algae" @default.
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- W2088468983 doi "https://doi.org/10.1111/j.1399-3054.1971.tb06715.x" @default.
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