作者: Martin Bähler , Hans M. Eppenberger , Theo Wallimann
DOI: 10.1016/0022-2836(85)90112-3
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摘要: A new thick-filament-associated protein, the 86 kd of chicken pectoralis major muscle was isolated from a crude C-protein preparation by method similar to that used purify H-protein rabbit skeletal muscle. However, protein with an apparent Mr 86,000 and 370,000 as estimated gel electrophoresis permeation, respectively, is not related differs its elution behaviour hydroxyapatite columns, molecular weight, ultraviolet light spectrum, amino acid composition localization, amount present in myofibrils. The reveals high content proline permeation indicates either highly asymmetric or polymeric structure molecule. Antibodies raised rabbits against were demonstrated double immunodiffusion immunoblotting experiments be specific for this protein. They show no cross-reactivity any other myofibrillar muscle, e.g. myosin, M-band proteins, titin C-protein, nor did they exhibit significant crossreactivity rabbit. which has been purified also antibody affinity chromatography freshly prepared Guba-Straub extract washed myofibrils, component located within each half A-band.