Yazawa M, Sakuma M, Yagi K
J Biochem. 1980 May;87(5):1313-20. doi: 10.1093/oxfordjournals.jbchem.a132869.
Invertebrate calmodulins of the sea anemone and scallop muscle were isolated and their properties were compared with those of vertebrate calmodulins from rabbit muscle and pig brain. The molecular weights estimated by SDS-polyacrylamide gel electrophoresis were similar to the molecular weight (16,500) of the vertebrate calmodulins. Every calmodulin contained 1 mol each of trimethyllysine and histidine, and high contents of acidic amino acids. The marine invertebrate calmodulins contained only one tyrosine in contrast to two tyrosines in the vertebrate ones. As a result, the UV absorption spectra were clearly different. The Ca2+-induced difference UV absorption spectra of the invertebrate calmodulins were indistinguishable from those of the vertebrate ones in spite of the difference in tyrosine contents. In tryptic peptide maps of invertebrate calmodulins, a few spots different from those of vertebrate calmodulins were observed in the basic and acidic peptide regions. The calmodulins of invertebrate muscles and that of rabbit skeletal muscle were almost indistinguishable in terms of the activation profile of rabbit skeletal myosin light chain kinase.
分离出海葵和扇贝肌肉中的无脊椎动物钙调蛋白，并将它们的性质与来自兔肌肉和猪脑的脊椎动物钙调蛋白的性质进行比较。通过SDS-聚丙烯酰胺凝胶电泳估计的分子量与脊椎动物钙调蛋白的分子量（16,500）相似。每种钙调蛋白都含有1摩尔的三甲基赖氨酸和组氨酸，以及高含量的酸性氨基酸。与脊椎动物钙调蛋白含有两个酪氨酸不同，海洋无脊椎动物钙调蛋白仅含有一个酪氨酸。因此，紫外吸收光谱明显不同。尽管酪氨酸含量存在差异，但无脊椎动物钙调蛋白的Ca2+诱导差异紫外吸收光谱与脊椎动物的无法区分。在无脊椎动物钙调蛋白的胰蛋白酶肽图中，在碱性和酸性肽区域观察到一些与脊椎动物钙调蛋白不同的斑点。就兔骨骼肌肌球蛋白轻链激酶的激活情况而言，无脊椎动物肌肉的钙调蛋白与兔骨骼肌的钙调蛋白几乎无法区分。
