Studies on sarcoplasmic reticulum from slow-twitch muscle
Studies on sarcoplasmic reticulum from slow-twitch muscle
复制标题
慢肌肌浆网的研究
DOI:
10.1007/bf00711942
复制
发表时间:
1982
影响因子:
2.7
通讯作者:
M. G. Sarzała
中科院分区:
文献类型:
--
作者:
E. Zubrzycka;B. Korczak;H. Osińska;M. G. Sarzała
SummaryVesicles were isolated from membranes of the sarcoplasmic reticulum (SR) of rabbit slow-twitch muscle by differential and sucrose density gradient centrifugation after homogenization. In some experiments, the vesicles were further fractionated by loading them with calcium oxalate followed by centrifugation in a sucrose density gradient.Protein composition of the isolated vesicles was complex and differed from the protein composition of fast-twitch muscle vesicles. However, other protein components, which were also present in fast-twitch muscle SR vesicles, have been identified: Ca2+-dependent ATPase, calsequestrin, 160 000 molecular weight glycoprotein and 53 000 molecular weight glycoprotein. The amount of the Ca2+-dependent ATPase and calsequestrin was several times lower in the slow-twitch muscle SR vesicles. This has been observed in both the original and the loaded vesicles.The slow-twitch muscle SR vesicles showed active calcium transport, Ca2+-dependent ATPase activity, and the formation of the phosphorylated intermediate under conditions similar to those established for fast-twitch muscle SR. However, these activities, when expressed per mg of total protein, were several times lower than the analogous activities in the SR vesicles isolated from fast-twitch skeletal muscle. When the same enzyme activities were expressed per mg of the 105 000 molecular weight ATPase, the values obtained were very similar in both kinds of vesicles.The results indicate that the slow rate of calcium transport, found in slow-twitch muscle SR vesicles, may be related to a low content of the calcium-transporting ATPase in the membrane.
影响因子:
6.5
作者:
W. R. Morrison;L. Smith
通讯作者:
W. R. Morrison;L. Smith