Puistola U
Biochem J. 1982 Jan 1;201(1):215-9. doi: 10.1042/bj2010215.
Crude preparations of lysyl hydroxylase were extracted from chick-embryo tendons synthesizing exclusively type I collagen, chick-embryo sterna synthesizing exclusively type II collagen and HT-1080 sarcoma cells synthesizing exclusively type IV collagen. No differences were found in the Km values for Fe2+, 2-oxoglutarate and ascorbate between these three enzymes preparations. Similarly no differences were found in the Km values for type I and type II protocollagens and the rate at which type IV protocollagen is hydroxylated between these enzyme preparations. The extent to which type I protocollagen could be hydroxylated by the three enzymes was likewise identical. These data strongly argue against the existence of collagen-type-specific lysyl hydroxylase isoenzymes.
从仅合成I型胶原蛋白的鸡胚肌腱、仅合成II型胶原蛋白的鸡胚胸骨以及仅合成IV型胶原蛋白的HT - 1080肉瘤细胞中提取赖氨酰羟化酶的粗制品。在这三种酶制品中，Fe2 +、2 - 氧代戊二酸和抗坏血酸的Km值没有差异。同样，在这些酶制品中，I型和II型原胶原蛋白的Km值以及IV型原胶原蛋白的羟化速率也没有差异。这三种酶对I型原胶原蛋白的羟化程度同样相同。这些数据有力地反驳了存在胶原蛋白类型特异性赖氨酰羟化酶同工酶的观点。
