牛弹性蛋白中交联位点C端的氨基酸序列。
Amino acid sequences C-terminal to the cross-links in bovine elastin.
作者信息
Baig K M, Vlaovic M, Anwar R A
出版信息
Biochem J. 1980 Mar 1;185(3):611-6. doi: 10.1042/bj1850611.
All the desmosine-containing elastolytic peptides of bovine ligamentum-nuchae elastin have now been examined for amino acid sequences C-terminal to the cross-links. In addition, amino acid residues C-terminal to lysine residues in bovine tropoelastin were also examined. No tyrosine C-terminal to cross-links in bovine elastin or C-terminal to lysine in tropoelastin was detected. Apparently all the tyrosine residues C-terminal to lysine residues in pig tropoelastin are replaced with phenylalanine in bovine tropoelastin. All the data presented are consistent with the scheme proposed for the formation of desmosine and isodesmosine cross-links of elastin by Gerber & Anwar [(1975) Biochem. J. 149, 685--695].
目前已对牛项韧带弹性蛋白中所有含锁链素的弹性溶解肽进行了检测，以确定交联点C端的氨基酸序列。此外，还检测了牛原弹性蛋白中赖氨酸残基C端的氨基酸残基。在牛弹性蛋白的交联点C端或原弹性蛋白中赖氨酸的C端均未检测到酪氨酸。显然，猪原弹性蛋白中赖氨酸残基C端的所有酪氨酸残基在牛原弹性蛋白中都被苯丙氨酸取代。所呈现的所有数据都与Gerber和Anwar提出的弹性蛋白中锁链素和异锁链素交联形成的方案一致[（1975年）《生物化学杂志》149卷，685 - 695页]。
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