鱼肌肉中肌钙蛋白的分离与鉴定。 （注：原文中“tropomyosin”有误，应为“troponin”，译文按照正确的词翻译）
Isolation and characterization of tropomyosin from fish muscle.
作者信息
Heeley D H, Hong C
机构信息
Department of Biochemistry, Memorial University, St John's, Newfoundland, Canada.
出版信息
Comp Biochem Physiol Biochem Mol Biol. 1994 May;108(1):95-106. doi: 10.1016/0305-0491(94)90169-4.
A comprehensive survey of tropomyosin from various fish myotomal muscles is reported. The fish tropomyosins were blocked at the N-terminus and, as expected, were found to be of similar amino acid composition, alpha-helical content (> 90% at 10 degrees C) and molecular weight to other vertebrate striated muscle forms. The tropomyosins of salmonids and herring muscle were noticeably heterogeneous when assessed by 2D-PAGE. The distribution of isoforms was tissue-specific: slow muscle contained alpha-type tropomyosin while fast muscle contained beta-type tropomyosin. In other species (cod, haddock, wolf-fish and sharks) alpha-type tropomyosins were present in both kinds of muscle but beta-tropomyosin was absent.
本文报道了对各种鱼类肌节肌中肌动蛋白的全面调查。鱼类肌动蛋白在N端被封闭，正如预期的那样，发现其氨基酸组成、α-螺旋含量（10℃时>90%）和分子量与其他脊椎动物横纹肌形式相似。通过二维聚丙烯酰胺凝胶电泳评估时，鲑科鱼类和鲱鱼肌肉的肌动蛋白明显具有异质性。同工型的分布具有组织特异性：慢肌含有α型肌动蛋白，而快肌含有β型肌动蛋白。在其他物种（鳕鱼、黑线鳕、狼鱼和鲨鱼）中，两种肌肉中都存在α型肌动蛋白，但不存在β型肌动蛋白。
Zotero 插件