| Literature DB >> 7026543 |
K Maruyama, M Kimura, S Kimura, K Ohashi, K Suzuki, N Katunuma.
Abstract
The effects of various proteolytic enzymes on the high molecular weight protein (connectin) present in a direct sodium dodecyl sulfate extract of myofibrils from chicken breast muscle were studied in detail. To keep the high molecular weight proteins intact, myofibrils had to be prepared in the presence of EGTA. Trypsin, chymotrypsin, papain, and nagarse readily hydrolyzed connectin (doublet band of titin) and the band 3 protein (N2-line protein). Pepsin did not attack connectin, but digested the band 3 protein and myosin. Calcium-activated neutral proteinase hydrolyzed the band 3 protein, leaving connectin intact. On the other hand, serine protease digested connectin but not the band 3 protein.Entities:
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Year: 1981 PMID: 7026543 DOI: 10.1093/oxfordjournals.jbchem.a133250
Source DB: PubMed Journal: J Biochem ISSN: 0021-924X Impact factor: 3.387