Proteolytic activity of proteasome on myofibrillar structures
作者: Richard G. TaylorCaroline TassyMariele BriandNathalie RobertYves BriandAhmed Ouali
作者单位: 1Station de Recherche sur la Viande, INRA
2Laboratoire de Biochimie, Université Blaise Pascal
刊名: Molecular Biology Reports, 1995, Vol.21 (1), pp.71-73
来源数据库: Springer Nature Journal
DOI: 10.1007/BF00990974
关键词: muscle fibermyofibrilproteasomeproteolysis
英文摘要: Abstract(#br)The physiologic function of proteasome remains unclear. Evidence suggests a role in degradation of ubiquitin-protein conjugates, MHC antigen presentation, and some specificity of substrate within certain cell types. To explore further the properties of proteasome we have examined its effect on a well defined structure, the myofibril. We find that despite its large size (20S) proteasome is able to degrade myofibrils and intact, permeabilized muscle fibrils. The proteins degraded showed some specificity because actin, myosin and desmin were degraded faster than α-actinin, troponin T and tropomyosin. Changes in ultrastructure were slow and included a general loss of structure with Z and I bands effected before the M band and costameres.
全文获取路径: Springer Nature  (合作)
影响因子:2.506 (2012)

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