The effect of proteasome on myofibrillar structures in bovine skeletal muscle |
| |
Authors: | Robert N Briand M Taylor R Briand Y |
| |
Affiliation: | Université Blaise Pascal, Clermont II, Laboratoire de Biochimie Appliquée, 63177 Aubiere Cedex, France. |
| |
Abstract: | When bovine myofibrils are incubated with the 20S proteasome their structure is rapidly damaged with loss of material, particularly from the Z discs and I bands. After 24 hr of incubation the myofibrils rupture and debris appears. Certain myofibrillar proteins, including nebulin, myosin, actin and tropomyosin, are hydrolysed during the incubation; others are solubilised (α-actinin). The 20S proteasome completely and rapidly hydrolyses purified myofibrillar proteins in an energy-independent manner. This shows that the 20S proteasome probably plays a role in the postmortem transformation of muscle and more generally in the hydrolysis of cellular proteins.(1). |
| |
Keywords: | |
本文献已被 ScienceDirect PubMed 等数据库收录! |
|