| Literature DB >> 914785 |
K Maruyama, S Kimura, M Kuroda, S Handa.
Abstract
Pure myofibrils were isolated from bovine heart by sucrose layer ultracentrifugation. Cardiac myofibrils thus prepared contained more protein as insoluble stroma than skeletal muscle. The insoluble stroma largely consisted of connectin, an elastic protein of muscle. The connectin content in cardiac myofibrils was about 18% of the total myofibrillar protein and was three times that in skeletal myofibrils. In view of the role of connectin as an elastic component of muscle, the abundance of connectin in cardiac myofibrils may be responsible for keeping myofibrils short at rest. This would account for the more effective tension generation in cardiac muscle on passive stretching due to blood inflow (Stirling's law).Entities:
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Year: 1977 PMID: 914785
Source DB: PubMed Journal: J Biochem ISSN: 0021-924X Impact factor: 3.387