Title: Metabolism of the reserve polysaccharide of Streptococcus mitis
Abstract: A maltodextrin phosphorylase found in cell extracts of several strains of Streptococcus mitis has been purified and freed from several other enzymes concerned with glycogen synthesis and degradation. Maltodextrins were the best primers for the synthetic reaction; glycogen was a poor primer for this phosphorylase. Further indications that the enzyme was not a glycogen phosphorylase were (i) its lack of binding with glycogen, (ii) the high Km value for glycogen which was 130-fold higher than that of muscle phosphorylase, (iii) the low rate of phosphorolysis of glycogen, and (iv) the low limit of conversion of glycogen into d-glucopyranosyl phosphate. A second phosphorylase was found with particulate glycogen in the pellet obtained on centrifuging sonicated cells. This was considered to be the enzyme involved in the degradation of glycogen.
Publication Year: 1969
Publication Date: 1969-04-01
Language: en
Type: article
Indexed In: ['crossref']
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Cited By Count: 6
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