Differences between glycogen synthases from rat and rabbit skeletal muscle as indicated by phosphopeptide maps.
Differences between glycogen synthases from rat and rabbit skeletal muscle as indicated by phosphopeptide maps.
复制标题
磷酸肽图显示大鼠和兔骨骼肌糖原合酶之间的差异。
DOI：
10.1016/0167-4889(87)90144-3
复制
发表时间：
1987
期刊：
影响因子：
--
通讯作者：
E. Reimann
中科院分区：
文献类型：
--
作者：
M. Hegazy;K. K. Schlender;E. Reimann
糖原合成酶I是从大鼠骨骼肌中纯化的。在十二烷基硫酸钠聚丙烯酰胺凝胶电泳上，酶作为一个主带迁移，亚单位mr85000。比活性（24单位/毫克蛋白质）、活性比（无葡萄糖-6- p100时的活性除以有葡萄糖-6- p100时的活性）（92±2）和磷酸含量（0.6 mol/mol亚单位）与兔骨骼肌酶相似。酪蛋白激酶I、酪蛋白激酶II（糖原合成酶激酶5）、糖原合成酶激酶3（激酶FA）、糖原合成酶激酶4、磷酸化酶激酶以及camp依赖性蛋白激酶的催化亚基对大鼠肌糖原合成酶的磷酸化和失活与兔肌合成酶相似。在酪蛋白激酶1磷酸化糖原合成酶后，大鼠肌糖原合成酶活性下降幅度最大。通过CNBr、胰蛋白酶或凝乳胰蛋白酶消化不同32p标记形式的糖原合成酶，获得糖原合成酶的磷酸肽图。采用十二烷基硫酸钠聚丙烯酰胺凝胶电泳法分离CNBr肽段，反相高效液相色谱法分离胰蛋白酶肽段和凝乳蛋白酶肽段。虽然大鼠和兔的合成酶形式给出了相似的肽图，但兔糖原合成酶n端区衍生的磷酸肽与推测来自大鼠糖原合成酶n端区相应的肽之间存在显著差异。对于CNBr肽，大鼠的明显mr值为12500，家兔为12000。两种植物获得的色氨酸保留时间不同。由大鼠骨骼肌糖原合成酶经磷酸化酶激酶磷酸化得到一个糜胰肽，而由兔酶磷酸化得到两个糜胰肽。这些结果表明，兔糖原合成酶的n端含有四个可磷酸化残基(Kuret et al. (1985) Eur。与大鼠糖原合成酶的n端不同。生物化学，151,39-48)。
Glycogen synthase I was purified from rat skeletal muscle. On sodium dodecyl sulfate polyacrylamide gel electrophoresis, the enzyme migrated as a major band with a subunitMrof 85 000. The specific activity (24 units/mg protein), activity ratio (the activity in the absence of glucose-6-Pdivided by the activity in the presence of glucose-6-P× 100) (92 ± 2) and phosphate content (0.6 mol/mol subunit) were similar to the enzyme from rabbit skeletal muscle. Phosphorylation and inactivation of rat muscle glycogen synthase by casein kinase I, casein kinase II (glycogen synthase kinase 5), glycogen synthase kinase 3 (kinase FA), glycogen synthase kinase 4, phosphorylasebkinase, and the catalytic subunit of cAMP-dependent protein kinase were similar to those reported for rabbit muscle synthase. The greatest decrease in rat muscle glycogen synthase activity was seen after phosphorylation of the synthase by casein kinase I. Phosphopeptide maps of glycogen synthase were obtained by digesting the different32P-labeled forms of glycogen synthase by CNBr, trypsin, or chymotrypsin. The CNBr peptides were separated by sodium dodecyl sulfate polyacrylamide gel electrophoresis and the tryptic and chymotryptic peptides were separated by reversed-phase HPLC. Although the rat and rabbit forms of synthase gave similar peptide maps, there were significant differences between the phosphopeptides derived from the N-terminal region of rabbit glycogen synthase and the corresponding peptides presumably derived from the N-terminal region of rat glycogen synthase. For CNBr peptides, the apparentMrwas 12 500 for rat and 12 000 for the rabbit. The tryptic peptides obtained from the two species had different retention times. A single chymotryptic peptide was produced from rat skeletal muscle glycogen synthase after phosphorylation by phosphorylase kinase whereas two peptides were obtained with the rabbit enzyme. These results indicate that the N-terminus of rabbit glycogen synthase, which contains four phosphorylatable residues (Kuret et al. (1985) Eur. J. Biochem. 151, 39–48), is different from the N-terminus of rat glycogen synthase.
登录
查看更多内容
DOI：
--
发表时间：
1983
期刊：
The Journal of biological chemistry
影响因子：
--
作者：
DePaoli-Roach,AA;Ahmad,Z;Camici,M;LawrenceJr,JC;Roach,PJ
通讯作者：
Roach,PJ
糖原合酶激酶的磷酸化位点特异性：使用高效液相色谱进行肽图测定。
影响因子：
3.9
作者：
Juhl,H;Sheorain,VS;Schworer,CM;Jett,MF;Soderling,TR
通讯作者：
Soderling,TR
大鼠骨骼肌糖原合酶：纯化酶被 cAMP 依赖性和非依赖性蛋白激酶磷酸化。
影响因子：
3.9
作者：
Hiken,JF;LawrenceJr,JC
通讯作者：
LawrenceJr,JC
能够磷酸化糖原合成酶和卵黄高磷蛋白的兔骨骼肌蛋白激酶 (PC0.7) 的表征。
DOI：
--
发表时间：
1981
期刊：
The Journal of biological chemistry
影响因子：
--
作者：
DePaoli-Roach,AA;Ahmad,Z;Roach,PJ
通讯作者：
Roach,PJ
DOI：
--
发表时间：
1984
期刊：
The Journal of biological chemistry
影响因子：
--
作者：
Ahmad,Z;Camici,M;DePaoli-Roach,AA;Roach,PJ
通讯作者：
Roach,PJ