Brewer J M, Arnold J, Beach G G, Ragland W L, Wunderlich J K
Department of Biochemistry, University of Georgia, Athens 30602.
Biochem Biophys Res Commun. 1991 Nov 27;181(1):226-31. doi: 10.1016/s0006-291x(05)81406-8.
Chicken leg muscle parvalbumin was digested with cyanogen bromide or trypsin or trypsin after citraconylation. Peptides isolated by reverse phase HPLC at pH 7.0 were subjected to acid hydrolysis and amino acid analysis and, in some cases, sequencing. The chicken muscle parvalbumin amino acid sequence has ca. 80% sequence identity with alpha-type parvalbumins from mammalian (rabbit, human and rat) muscle. By contrast, the chicken thymus parvalbumin ("avian thymic hormone") sequence is very similar to reptile (turtle, salamander and frog) muscle beta-type parvalbumins. We hypothesize that the evolutionary appearance of the warm-blooded reptiles was accompanied by recruitment of the beta parvalbumin isozyme for promotion of lymphocyte maturation.
鸡腿肌肉中的小清蛋白用溴化氰、胰蛋白酶或柠康酰化后再用胰蛋白酶进行消化。在pH 7.0条件下通过反相高效液相色谱法分离得到的肽段进行酸水解和氨基酸分析，在某些情况下还进行测序。鸡肌肉小清蛋白的氨基酸序列与哺乳动物（兔、人和大鼠）肌肉中的α型小清蛋白约有80%的序列同一性。相比之下，鸡胸腺小清蛋白（“禽胸腺激素”）的序列与爬行动物（龟、蝾螈和蛙）肌肉中的β型小清蛋白非常相似。我们推测，温血爬行动物的进化出现伴随着β小清蛋白同工酶的募集，以促进淋巴细胞成熟。
