作者: N Nakayama , T L Kirley , P L Vaghy , E McKenna , A Schwartz
DOI: 10.1016/S0021-9258(18)48279-8
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摘要: A putative Ca2+ channel protein was purified from rabbit skeletal muscle transverse tubules with the combined use of lectin affinity chromatography and ion-exchange chromatography, followed by sucrose density gradient centrifugation. The major component preparation detected sodium dodecyl sulfate-gel electrophoresis a 150 kDa when reduced 20 mM dithiothreitol 191-kDa treated N-ethylmaleimide. Therefore, this appears to be identical alpha subunit previously described (Curtis, B. M., Catterall, W. A. (1984) Biochemistry 23, 2113-2118). This preparative electrophoresis, electroelution and/or electroblotting, its amino acid composition NH2-terminal sequence were determined. is: NH2-Glu-Pro-Phe-Pro-Ser-Ala-Val-X-Ile-Lys-Ser-X-Val-X-Lys-Met-Gln-.