Mammalian skeletal muscle C-protein: purification from bovine muscle, binding to titin and the characterization of a full-length human cDNA.

摘要: We report a fast method for the isolation of homogeneous C-protein from bovine skeletal muscle. In electron micrographs appears as short rods with relatively uniform length about 50 nm. Protein sequencing shows single N-terminal sequence. Radio-labelled strongly decorates titin II and myosin but not heads. Binding to is retained in preparations lacking titin-associated proteins. Antibodies were used screen lambda gt11 cDNA library constructed fetal human Clone HC38 3833 bp long encodes protein 1138 amino acid residues. The start predicted sequence fits protein. All partial sequences obtained (348 residues) deduced chicken (Einheber Fischman, 1990) can be aligned along C-proteins share 50% identity 70% similarity. Along repeat patterns fibronectin (Fn)-like domains are better conserved than immunoglobulin (Ig)-like domains. Regions strong divergence between slow may represent differences isoforms.