作者: H. Negishi , E. Yamamoto , T. Kuwata
DOI: 10.1016/0309-1740(95)00044-5
关键词: Polyclonal antibodies 、 Ageing 、 Troponin T 、 Proteolysis 、 Biochemistry 、 Myofibril 、 Troponin 、 Antibody 、 Protein subunit 、 Chemistry
摘要: Abstract The most predominant component appearing on SDS-PAGE of myofibrils prepared from bovine m. vastus intermedius (VI) during ageing for 31 days post mortem at 0–2 °C was a with molecular weight 32 kDa (SDS-32 kDa). In this study, the origin SDS-32 component, which thought to correspond 30 already known, investigated. On crude troponins, both troponin T and 34 were gradually degraded then disappeared 24 , while concentration showed tendency increase ageing. VI muscle stored 17 using CM-Toyopearl chromatography, named native component. Its mobility agreed that SDS-32, components recognized by polyclonal anti-troponin antibody, furthermore, patterns amino acid composition very similar T. Thus, it considered these two would be polypeptides degradation We concluded must derived poly-peptides However, still remains possibility some products other myofibrillar proteins are included in Therefore, further studies about identity will required.