Frillingos S, Frangou-Lazaridis M, Seferiadis K, Hulmes J D, Pan Y C, Tsolas O
Laboratory of Biological Chemistry, University of Ioannina Medical School, Greece.
Mol Cell Biochem. 1991 Nov 13;108(1):85-94. doi: 10.1007/BF00239545.
Goat prothymosin alpha, a highly acidic polypeptide of pI3.5, 109 amino acid residues, has been isolated from lymphoid and non-lymphoid tissues of young female goats. Unlike rat, murine and porcine prothymosins alpha, goat prothymosin alpha appears at a higher concentration in the spleen compared with the thymus. The sequence of segments of the polypeptide involving known mutations has been determined, by automatic sequencing of its tryptic peptide fragments. The acidic amino acid-rich segment in the middle of the molecule, including residues 49-83, has not been sequenced. Goat prothymosin alpha closely resembles bovine prothymosin alpha, with only one substitution, proline for alanine at position 85. It also resembles human prothymosin alpha, with only three substitutions. It differs more significantly from rat and murine prothymosins alpha, by two deletions and three substitutions. The results show the highly conserved nature of the molecule, with substitutions at given positions only.
山羊原胸腺素α是一种pI为3.5的高酸性多肽，由109个氨基酸残基组成，已从幼年雌性山羊的淋巴组织和非淋巴组织中分离出来。与大鼠、小鼠和猪的原胸腺素α不同，山羊原胸腺素α在脾脏中的浓度高于胸腺。通过对其胰蛋白酶肽片段进行自动测序，已确定了该多肽中涉及已知突变的片段序列。分子中间富含酸性氨基酸的片段，包括第49 - 83位残基，尚未测序。山羊原胸腺素α与牛原胸腺素α非常相似，仅在第85位有一个取代，即脯氨酸取代丙氨酸。它也与人类原胸腺素α相似，只有三个取代。它与大鼠和小鼠的原胸腺素α差异更为显著，有两个缺失和三个取代。结果表明该分子具有高度保守性，仅在特定位置发生取代。
