骨骼肌肌浆网中钙结合蛋白结合的30 kDa蛋白的生化特性

Biochemical characterization of calsequestrin-binding 30-kDa protein in sarcoplasmic reticulum of skeletal muscle.

作者信息

Kagari T, Yamaguchi N, Kasai M

机构信息

Department of Biophysical Engineering, Faculty of Engineering Science, Osaka University, Japan.

出版信息

Biochem Biophys Res Commun. 1996 Oct 23;227(3):700-6. doi: 10.1006/bbrc.1996.1572.

DOI:10.1006/bbrc.1996.1572

PMID:8885997

Abstract

Calsequestrin (CSQ)-binding 30-kDa protein in the sarcoplasmic reticulum (SR) of rabbit skeletal muscle was purified from the junctional face membrane (JFM) in the SR. Analysis of proteins which bound to the affinity column conjugated with the purified 30-kDa protein was performed. As a result, in the heavy fraction of the SR (HSR), four proteins including CSQ proved to be adsorbed on the column, and in the JFM, one protein, whose molecular weight was about 25-kDa. was mainly adsorbed. Furthermore, the same 25-kDa protein was found to be adsorbed on the CSQ affinity column. This 25-kDa protein is probably the CSQ-binding 26-kDa protein (junctin) recently reported [Jones, L. R., et al. (1995) J. Biol. Chem. 270, 30787] judging from the molecular weight and the CSQ-binding property. These results suggest that three proteins, CSQ, 30-kDa protein, and 25-kDa protein, form a protein complex in the terminal cisternae of the SR.

摘要

从兔骨骼肌肌浆网（SR）的连接面膜（JFM）中纯化出肌集钙蛋白（CSQ）结合的30 kDa蛋白。对与纯化的30 kDa蛋白偶联的亲和柱上结合的蛋白质进行了分析。结果显示，在SR的重质部分（HSR）中，包括CSQ在内的四种蛋白质被吸附在柱上，而在JFM中，一种分子量约为25 kDa的蛋白质主要被吸附。此外，发现相同的25 kDa蛋白质也被吸附在CSQ亲和柱上。从分子量和CSQ结合特性判断，这种25 kDa蛋白质可能是最近报道的CSQ结合的26 kDa蛋白质（连接蛋白）[琼斯，L.R.等人（1995年）《生物化学杂志》270，30787]。这些结果表明，CSQ、30 kDa蛋白和25 kDa蛋白这三种蛋白质在SR的终池形成了一个蛋白质复合物。