Collins D, Lindberg K, McLees B, Pinnell S
Biochim Biophys Acta. 1977 Nov 25;495(1):129-39. doi: 10.1016/0005-2795(77)90247-1.
A hydroxylysine-rich type I collagen has been isolated from pepsin-digested porcine heart valve. The ratio of alpha1 to alpha2 in the isolated molecule was 2:1. The component alpha chains exhibited unusual chromatographic behavior in comparison to corresponding chains from human dermis and lathyritic rat skin collagen. The composition of component cyanogen bromide peptides identified the alpha chains as authentic type I chains and demonstrated hydroxylysine enrichment throughout the length of the chain. delta6-Dehydro-5,5'dihydroxylysinonorleucine, a collagen cross-link derived from two hydroxylysyl residues and ordinarily found in hard tissue collagens was found to be the predominant cross-link in heart valve.
一种富含羟赖氨酸的I型胶原蛋白已从经胃蛋白酶消化的猪心脏瓣膜中分离出来。分离出的分子中α1与α2的比例为2:1。与来自人真皮和患骨生成障碍大鼠皮肤胶原蛋白的相应链相比,组成成分的α链表现出异常的色谱行为。溴化氰肽成分的组成确定α链为正宗的I型链,并证明链的全长都富含羟赖氨酸。δ6-脱氢-5,5'-二羟基赖氨酰正亮氨酸是一种由两个羟赖氨酰残基衍生而来的胶原蛋白交联物,通常存在于硬组织胶原蛋白中,它被发现是心脏瓣膜中的主要交联物。