Csizmadia A M, Bonet-Kerrache A, Nyitray L, Mornet D
Department of Biochemistry, Eötvös Lorand University, Budapest, Hungary.
Comp Biochem Physiol Biochem Mol Biol. 1994 May;108(1):59-63. doi: 10.1016/0305-0491(94)90165-1.
In this comparative study, the heat-stable protein content of scallop muscles was reinvestigated. The hCaD-like protein was prepared and its properties carefully examined. The heat-stable high-molecular-mass caldesmon-like (hCaD-like) protein is only present in the catch (smooth) muscle and it is completely absent in the striated muscle of scallop. The isolated scallop hCaD-like protein cosediments with F-actin, binds to myosin significantly and inhibits the ATPase activity of acto-myosin. A partial cDNA clone from a Mytilus anterior byssus retractor muscle (ABRM)-related protein showed strong homology with the hCaD gizzard sequence. This allowed identification of the heat-stable 100-110 kDa protein doublet band isolated in this study as a caldesmon-like molecule.
在这项比较研究中，对扇贝肌肉的热稳定蛋白含量进行了重新研究。制备了类hCaD蛋白并仔细检查了其特性。热稳定的高分子量类钙调蛋白（hCaD样）蛋白仅存在于扇贝的闭壳（平滑肌）中，而在扇贝的横纹肌中则完全不存在。分离得到的扇贝hCaD样蛋白与F-肌动蛋白共沉降，与肌球蛋白有显著结合，并抑制肌动球蛋白的ATP酶活性。来自贻贝前足丝牵缩肌（ABRM）相关蛋白的部分cDNA克隆与hCaD砂囊序列有很强的同源性。这使得本研究中分离出的热稳定的100-110 kDa蛋白双峰带被鉴定为类钙调蛋白分子。
