Endogenous phosphates on liver glycogen synthase D and synthase I. Studies on the number and location.
نویسندگان
چکیده
منابع مشابه
Presence of an intermediate synthase form during the conversion of glycogen synthase D into synthase I in rat liver extract.
When synthase D was converted into synthase I in a liver extract, it progressed through a synthase form with activity characteristics that could not be explained by a mixture of the original synthase D and the final product, synthase I. This form was distinguished by an affinity for UDP-glucose, in the absence of glucose 6-phosphate, which was intermediate between those of the two known forms.
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Limited tryptic digestion of either synthase I or D forms resulted in the appearance of a new glucose 6-phosphate-dependent form which was composed of 75,000 molecular weight subunits. Early in tryptic digestion, an intermediate 78,000 subunit was also observed with both forms of the enzyme. The NH,terminal dipeptide sequence of the 75,000 subunit of both forms was the same as that of the origi...
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A rabbit liver protein kinase (PCO.,), able to phosphorylate glycogen synthase and phosvitin, has been extensively purified. The enzyme had apparent M, = 170,000-190,000 as judged by gel filtration and was associated with two major polypeptide species, a (Mr = 43,000) and lp (Mr = 25,000). Two other polypeptides, Mr = 38,000 and M, = 35,000, were also detected. Treatment with trypsin led to an...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1983
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(17)44542-x