Calmodulins from muscles of marine invertebrates, scallop and sea anemone.
Calmodulins from muscles of marine invertebrates, scallop and sea anemone.
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来自海洋无脊椎动物、扇贝和海葵肌肉的钙调蛋白。
DOI：
10.1093/oxfordjournals.jbchem.a132869
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发表时间：
1980
影响因子：
2.7
通讯作者：
K. Yagi
中科院分区：
文献类型：
--
作者：
M. Yazawa;M. Sakuma;K. Yagi
从海葵和扇贝肌肉中分离出无脊椎动物钙调素，并与兔肌肉和猪脑中的脊椎动物钙调素的性质进行了比较。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素的分子量（16，500）相似。每个钙调素含有1摩尔的三甲基赖氨酸和组氨酸，并含有高含量的酸性氨基酸。海洋无脊椎动物的钙调素只含有一个酪氨酸，而脊椎动物的钙调素含有两个酪氨酸。结果，UV吸收光谱明显不同。无脊椎动物钙调素的钙离子诱导的差异紫外吸收光谱是无法区分的脊椎动物的，尽管在酪氨酸含量的差异。在无脊椎动物钙调素的胰蛋白酶肽图中，在碱性和酸性肽区观察到一些不同于脊椎动物钙调素的点。无脊椎动物肌肉和兔骨骼肌的钙调素在兔骨骼肌肌球蛋白轻链激酶的激活谱方面几乎是不可区分的。
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.