Aspects of the Animal Collagenases
Aspects of the Animal Collagenases
复制标题
动物胶原酶的各个方面
DOI：
--
复制
发表时间：
1976
期刊：
影响因子：
--
通讯作者：
J. Gross
中科院分区：
文献类型：
--
作者：
J. Gross
自第一个动物胶原酶被检测到以来，过去13年来积累的信息（Gross和Lapiere，1962年; Lapiere和Gross，1963）指出，生物系统中的胶原蛋白溶解是通过一系列酶完成的，其中一种酶在细胞外空间中的生理pH和温度下操作，在原纤维内的分子螺旋体中产生第一个和关键的断裂（Gross和永井，1965; Kang等人，1966年; Sakai和Gross，1967年）。该步骤之后是一种或多种酶活性，其将多肽片段还原成更小的肽和氨基酸。我们对负责最初攻击的酶的了解要比我们对随后的碎片分解的了解多得多。后一系列事件中有多少发生在细胞内还有待确定。分子末端非螺旋区域内的肽键初步切割导致不溶性原纤维中分子间交联丧失的可能性是真实的，但尚未明确检测到中性pH下的这种酶活性。
Information accumulated over the past 13 years since the first animal collagenase was detected (Gross and Lapiere, 1962; Lapiere and Gross, 1963) indicates that collagenolysis in biological systems is accomplished by a series of enzymes one of which, operating at physiologic pH and temperature in the extracellular spaces, produces the first and critical cleavage in the helical body of the molecule within the fibril (Gross and Nagai, 1965; Kang et al., 1966; Sakai and Gross, 1967). This step is followed by one or more enzyme activities which reduce the polypeptide fragments to smaller peptides and amino acids. We know considerably more about the enzyme responsible for the initial attack than we do about subsequent dismantling of the fragments. How much of this latter series of events takes place within the cell has yet to be determined. The possibility of a preliminary cleavage of peptide bonds within the terminal nonhelical regions of the molecule resulting in loss of intermolecular cross-linking in insoluble fibrils is a real one, but such an enzyme activity at neutral pH has not yet been unequivocally detected.