Rich E A, Seyer J M, Kang A H, Mainardi C L
Am Rev Respir Dis. 1983 Jul;128(1):166-9. doi: 10.1164/arrd.1983.128.1.166.
An enzyme capable of degrading type V collagen was found in the sputum of patients with chronic obstructive pulmonary disease (COPD). This enzyme was found in a latent form and was activated by 4-aminophenylmercuric acetate (APMA). Molecular sieve chromatography on Ultrogel AcA-34 and affinity chromatography on type V collagen-Sepharose were successful in separating type V from type I collagenolytic activity. The enzyme became active after affinity chromatography and no longer required activation with APMA to manifest activity. It was found to be a metalloproteinase by virtue of its inhibition by ethylene-diaminetetraacetic acid and phenanthroline but not by phenylmethanesulfonyl fluoride or N-ethylmaleimide. Because degradation of matrix proteins is felt to be important in the pathogenesis of COPD, it is possible that the selective degradation of type V collagen by this enzyme may play a role in the development of COPD.
在慢性阻塞性肺疾病（COPD）患者的痰液中发现了一种能够降解V型胶原的酶。该酶以潜伏形式存在，并被乙酸4-氨基苯汞（APMA）激活。使用Ultrogel AcA-34进行分子筛色谱分析以及使用V型胶原-琼脂糖进行亲和色谱分析成功地将V型胶原的分解活性与I型胶原的分解活性分离。该酶在亲和色谱后变得有活性，并且不再需要用APMA激活来表现活性。由于其受到乙二胺四乙酸和菲咯啉的抑制而不受苯甲基磺酰氟或N-乙基马来酰亚胺的抑制，因此发现它是一种金属蛋白酶。由于基质蛋白的降解被认为在COPD的发病机制中很重要，所以这种酶对V型胶原的选择性降解可能在COPD的发展中起作用。
