Mecham R P, Foster J A
Biochem J. 1978 Aug 1;173(2):617-25. doi: 10.1042/bj1730617.
Desmosine-enriched peptides were isolated from a thermolysin digest of bovine ligamentum nuchae elastin and a partial sequence was determined. A 'two-cross-link' model is proposed in which a second cross-link, perhaps lysinonorleucine, joins two peptide chains approx. 35 amino acid residues removed from the desmosine. Implied in this model is a certain asymmetry or directionality which places restrictions on the 'sense' of the peptide chains (either always parallel or anti-parallel) in order to align the cross-linking sites. Imposing such restrictions raises the possibility of specific alignment of elastin precursor molecules by microfibrillar proteins and/or aligning peptides on the precursor molecules themselves.
从牛项韧带弹性蛋白的嗜热菌蛋白酶消化物中分离出富含锁链素的肽段,并测定了部分序列。提出了一种“双交联”模型,其中第二个交联键(可能是赖氨酰正亮氨酸)连接两条肽链,距离锁链素约35个氨基酸残基。该模型意味着一定的不对称性或方向性,这对肽链的“方向”(始终平行或反平行)施加了限制,以便使交联位点对齐。施加这些限制增加了微原纤维蛋白和/或前体分子自身上的对齐肽对弹性蛋白前体分子进行特异性对齐的可能性。