Inhibition by collagen chains of lysyl hydroxylase of chick embryo and of WI-38 human lung fibroblasts. |
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Authors: | B Oppenheim S Englard |
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Institution: | Department of Biochemistry, Albert Einstein College of Medicine, Yeshiva University Bronx, New York, 10461 USA |
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Abstract: | Lysyl hydroxylase from chick embryos was strongly inhibited by heat-denatured collagens from various vertebrate sources, and by separated a chains and β components of rat tail tendon collagen. The kinetics exhibited with this enzyme when heat-denatured calf or rabbit skin collagens was used showed a mixed type of inhibition. On the other hand, a preparation of homologous heat-denatured 4,5-3H-L-lysine-labeled collagen, in itself an extremely poor substrate for the hydroxylase, showed non-competitive inhibition with a Ki of about 8–9 μM. Finally, the lysyl hydroxylase preparations from WI-38 fetal human lung fibroblasts and from transformed WI-38 cells (WI-38 VA 13) were also inhibited by heat-denatured collagens or, where tested, by separated collagen chains. |
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