Keutmann H T, Niall H D, O'Riordan J L, Potts J T
Biochemistry. 1975 May 6;14(9):1842-7. doi: 10.1021/bi00680a006.
The sequence of the amino-terminal portion of human parathyroid hormone, particularly the identity of residues 22, 28, and 30 (the subject of discrepancies in recent published reports), has been reexamined by two basic methods of structural analysis. A fresh lot of human parathyroid hormone isolated from pooled adenoma tissue was analyzed by Edman degradation with identification of critical residues by thin-layer chromatography and gas-liquid chromatography. In the second approach, -14C or tritiated amino acids were incorporated during biosynthesis of the human hormone in slices of parathyroid glands in vitro; the appropriate amino acid residues were then determined as the -14C or tritiated phenythiohydantoin derivatives of the amino acid after Edman degradation, or by peptide isolation after appropriate cleavage with endopeptidase, or both. The results confirm our previous findings that residue 22 is glutamic acid, residue 28 is leucine, and residue 30 is aspartic acid.
人类甲状旁腺激素氨基末端部分的序列，特别是第22、28和30位残基的身份（这是近期发表报告中存在差异的主题），已通过两种基本的结构分析方法重新进行了研究。从汇集的腺瘤组织中分离出一批新的人类甲状旁腺激素，通过埃德曼降解法进行分析，并通过薄层色谱法和气液色谱法鉴定关键残基。在第二种方法中，在体外甲状旁腺切片中人类激素的生物合成过程中掺入了-14C或氚标记的氨基酸；然后在埃德曼降解后，将适当的氨基酸残基确定为氨基酸的-14C或氚标记的苯硫基乙内酰脲衍生物，或者在使用内肽酶进行适当切割后通过肽分离来确定，或者两者兼用。结果证实了我们之前的发现，即第22位残基是谷氨酸，第28位残基是亮氨酸，第30位残基是天冬氨酸。
