COMPARISON OF CALREGULINS FROM VERTEBRATE LIVERS
COMPARISON OF CALREGULINS FROM VERTEBRATE LIVERS
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DOI：
10.1042/bj2420245
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发表时间：
1987-02-15
影响因子：
4.1
通讯作者：
WAISMAN, DM
中科院分区：
文献类型：
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作者：
KHANNA, NC;TOKUDA, M;WAISMAN, DM
从牛、兔和鸡肝中纯化钙调节蛋白，并比较它们的结构特性。三种钙调节蛋白之间的显着差异包括鸡钙调节蛋白 (57000) 的 Mr 值低于兔和牛钙调节蛋白 (63000)，以及仅牛钙调节蛋白的糖基化。三种钙调蛋白的氨基酸组成和肽图非常相似。三种蛋白质的 Ca2+ 结合特性没有检测到重大差异。 通过内在蛋白质荧光和疏水性荧光探针8-苯胺基-1-萘磺酸盐监测的Zn2+诱导的钙调蛋白构象和疏水性变化非常相似，表明牛、兔和鸡钙调蛋白的疏水性的Zn2+依赖性增加是保守的。这些研究更全面地定义了什么是钙调节蛋白，证明钙调节蛋白是脊椎动物肝脏中相对不变的成分，并表明钙调节蛋白结构在牛、鸡和兔肝脏中高度保守。
Calregulins were purified from bovine, rabbit and chicken liver, and their structural properties were compared. Significant differences between the three calregulins include a lower Mr for chicken calregulin (57000) than for rabbit and bovine calregulin (63000), and the glycosylation of only bovine calregulin. Amino acid compositon and peptide maps of the three calregulins were very similar. No major differences were detected in the Ca2+-binding properties of the three proteins. Zn2+-induced changes in calregulin conformation and hydrophobicity monitored by intrinsic protein fluorescence and the hydrophobic fluorescent probe 8-anilino-1-naphthelenesulphonate were very similar, suggesting that the Zn2+-dependent increase in the hydrophobicity of bovine, rabbit and chicken calregulin was conserved. These studies more fully define what is a calregulin, demonstrate that calregulin is a relatively invariant constituent of vertebrate liver, and indicate that calregulin structure has been highly conserved in bovine, chicken and rabbit liver.