Adipose Tissue Glycogen Synthetase

Barash, V.; Schramm, H; Gutman, Alisa

doi:10.1016/s0021-9258(19)43987-2

Cited by 16 publications

(2 citation statements)

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“…The sulfate and phosphate activation of swine adipose tissue glycogen synthase I is similar to the effects of these anions reported for glycogen synthase I from liver and muscle (Mersmann and Segal, 1967;Rosell-Perez and Villar-Palasi, 1964). In contrast, Barash et al (1973) reported that rat adipose tissue glycogen synthase, both the D and I forms, was inhibited by 5 mM inorganic phosphate, 5 mM Na2SC>4, or 20 mM KF. These results suggest that there may be significant differences between the rat and the swine adipose tissue enzymes.…”

Section: Discussionmentioning

confidence: 89%

“…Glycogen synthase from skeletal muscle (Soderling et al, 1970;Brown and Larner, 1971), heart (Thomas and Larner, 1973), liver (Lin and Segal, 1973), and kidney (Issa and Mendicino, 1973) has been purified to homogeneity and characterized. The enzyme from adipose tissue has not previously been purified, although some kinetic properties of the enzyme from adipose tissue crude homogenates have been reported (Barash et al, 1973). In order to study the hormonal regulation of glycogen synthase activity in adipose tissue it is necessary to obtain and characterize substrate quantities of the enzyme essentially free of its interconverting enzymes.…”

mentioning

confidence: 99%

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Enzymes regulating glycogen metabolism in swine subcutaneous adipose tissue. II. Glycogen synthase

Miller¹,

Miller²,

Fredholm³

et al. 1975

Biochemistry

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Glycogen synthase from swine adipose tissue was purified to apparent homogeneity using ethanol precipitation, DEAE chromatography, and affinity chromatography utilizing glucosamine 6-phosphate as the ligand. The purified enzyme migrated as a single protein component during electrophoresis on polyacrylamide gels at pH 7.3 although some protein failed to enter the running gel. Enzyme incubated with sodium dodecyl sulfate (SDS) migrated as one component (mol wt similar to 90,000) on SDS-polyacrylamide gel electrophoresis. The enzyme was relatively unstable at all stages of the purification procedure, but stability was increased in the presence of glucose 6-phosphate, UDPG, or glycerol. The isoelectric point of the purified enzyme and of enzyme activity in crude homogenates was pH 4.8. The sedimentation coefficient of the enzyme in crude homogenates was 8.5 S. The pH-activity profile showed an optimum at pH 7.8 in the absence of glucose 6-phosphate but no definable optimum between pH 7.0 and 9.2 in its presence. The Km of glycogen synthase I for UDPG was 250 muM in the absence and 37 muM in the presence of glucose 6-phosphate; the K-a for glucose 6-phosphate was 18 mu-M. The K-m of glycogen synthase D for UDPG was 130 mu-M in the presence of glucose 6-phosphate; the Ka for glucose 6-phosphate was 1 mM. The anions sulfate and phosphate activated the enzyme when assays were performed in the absence of glucose 6-phosphate. Fluoride produced activation of enzyme assayed either in the presence or in the absence of glucose 6-phosphate.

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Section: Discussionmentioning

confidence: 89%