Proteolytic activity in human skin fibroblasts harvested with trypsin and its effect on measurements of collagen hydroxylase activities. |
| |
Authors: | R S Quinn M Rosenblatt S M Krane |
| |
Institution: | 1. Department of Medicine, Harvard Medical School Massachusetts General Hospital, Boston, Massachusetts, 02114 USA;2. Medical Services (Arthritis and Endocrine Units) Massachusetts General Hospital, Boston, Massachusetts, 02114 USA |
| |
Abstract: | Lysates of human skin fibroblasts harvested without the use of trypsin do not contain detectable proteolytic activity, but when trypsin is used, lysates may contain activity equal to 10 ng of trypsin/107 cells. The amount of cell lysate ordinarily examined for collagen prolyl and lysyl hydroxylase activity is sufficiently small that such amounts of trypsin have no observable effect on the unhydroxylated collagen substrate. Larger amounts of trypsin cause proteolysis of the unhydroxylated collagen substrate and a reduction of both prolyl and lysyl hydroxylation with lysyl hydroxylation more affected at low trypsin concentration than prolyl hydroxylation. |
| |
Keywords: | |
本文献已被 ScienceDirect 等数据库收录! |
|