Gonzalez-Riopedre M, Barcia R, Ramos-Martínez J I
Department of Biochemistry and Molecular Biology, School of Veterinary, University of Santiago de Compostela, Campus of Lugo, 27002 Lugo, Spain.
Mol Cell Biochem. 2009 Jul;327(1-2):47-52. doi: 10.1007/s11010-009-0041-5. Epub 2009 Feb 13.
An enzyme that can be included into the so-called conventional PKCs has been purified to homogeneity from the mantle tissue of the sea mussel Mytilus galloprovincialis. This enzyme has a molecular weight of 60 kDa, which is DAG-dependent, PS-activated, and Ca2+-dependent. It was separated from a Ca2+-independent PKC (p105) (Mercado et al., Mol Cell Biochem 233:99-105, 2002) by means of an ionic exchange chromatography on DE-52 cellulose. The molecular weights and kinetic properties of both the enzymes are different. The protein p60 is broadly distributed among the tissues, which suggests that it may carry out specific functions, different from those performed by p105.
一种可归入所谓传统蛋白激酶C的酶已从地中海贻贝的外套膜组织中纯化至同质。这种酶的分子量为60 kDa，它依赖二酰甘油（DAG）、由磷脂酰丝氨酸（PS）激活且依赖钙离子（Ca2+）。通过在DE-52纤维素上进行离子交换色谱法，它与一种不依赖钙离子的蛋白激酶C（p105）（Mercado等人，《分子与细胞生物化学》233:99 - 105，2002年）分离。这两种酶的分子量和动力学特性不同。蛋白p60广泛分布于各组织中，这表明它可能执行与p105不同的特定功能。
