AT LEAST 6 DIFFERENT ACTINS ARE EXPRESSED IN A HIGHER MAMMAL - ANALYSIS BASED ON THE AMINO-ACID SEQUENCE OF THE AMINO-TERMINAL TRYPTIC PEPTIDE
AT LEAST 6 DIFFERENT ACTINS ARE EXPRESSED IN A HIGHER MAMMAL - ANALYSIS BASED ON THE AMINO-ACID SEQUENCE OF THE AMINO-TERMINAL TRYPTIC PEPTIDE
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DOI：
10.1016/0022-2836(78)90020-7
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发表时间：
1978-01-01
影响因子：
5.6
通讯作者：
WEBER, K
中科院分区：
文献类型：
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作者：
VANDEKERCKHOVE, J;WEBER, K
对不同牛组织中肌动蛋白氨基端色氨酸肽的蛋白质化学特征分析表明，该哺乳动物至少表达了6种不同的肌动蛋白结构基因。在骨骼肌肌动蛋白、心肌肌动蛋白、平滑肌肌动蛋白两种不同的肌动蛋白以及脑和胸腺等非肌肉组织的两种不同的肌动蛋白中发现了独特的氨基酸序列。在同一组织（如非肌肉组织和平滑肌）中存在不止一种肌动蛋白，这可以通过不同的氨基末端肽来证明，然而，它们是密切相关的。肌群肌（如骨骼肌和心肌）的肌动蛋白表现出独特但极其相似的氨基末端肽。牛和鸟类肌动蛋白涉及平滑肌和骨骼肌的有限比较强调，在高等脊椎动物中，肌动蛋白的差异涉及组织而不是物种特异性。对于低等真核生物，如多头绒泡菌，只发现一个肌动蛋白氨基末端肽，这表明在疟原虫阶段只有一种肌动蛋白存在。该肽的氨基酸序列虽然独特，但与相应的哺乳动物细胞质肌动蛋白肽具有高度的同源性。通过不同氨基末端肽的相对产率比较了不同的肌动蛋白提取和纯化方法。结果表明，通过目前的纯化程序获得的各种肌动蛋白物种是真实的反映实际存在于组织中的肌动蛋白。此外，我们比较了不同肌动蛋白的等电聚焦分析或不同肌动蛋白的氨基末端肽的蛋白质化学特征所提供的分辨率。我们发现后一种方法更适合记录肌动蛋白在进化和分化过程中的表达变化。
The protein chemical characterization of the amino-terminal tryptic peptide of actin from different bovine tissues shows that at least six different actin structural genes are expressed in this mammal.Unique amirio acid sequences are found for actin from skeletal muscle, for actin from heart muscle, for two different actin species from smooth muscle, and for two different actin species typical of non-muscle tissues such as brain and thymus. The presence of more than one actin species in the same tissue (e.g. nonmuscle tissues and smooth muscles) is demonstrated by different amino-terminal peptides which, however, are closely related. The actins from the sarcomeric muscles (e.g. skeletal muscle and heart muscle) show unique but extremely similar amino-terminal peptides. A limited comparison of bovine and avian actins involving smooth and skeletal muscles emphasizes that among higher vertebrates actin divergence involves tissue rather than species specificity.For the lower eukaryotic organismPhysarum polycephaluma single actin amino-terminal peptide is found, indicating that only one actin species is present during the plasmodial stage. The amino acid sequence of this peptide although unique reveals a high degree of homology with the corresponding mammalian cytoplasmic actin peptides.Different actin extraction and purification procedures have been compared by the relative yields of the different amino-terminal peptides. The results indicate that the various actin species obtained by the current purification procedures are a true reflection of the actual actins present in the tissue. In addition we compare the resolution provided by either isoelectric focusing analysis of different actins or by the protein chemical characterization of the amino-terminal peptides of different actins. We show that the latter procedure is more suitable for recording changes in actin expression during evolution and differentiation.