Mainardi C L, Hasty D L, Seyer J M, Kang A H
J Biol Chem. 1980 Dec 25;255(24):12006-10.
Purified polymorphonuclear leukocyte elastase degraded native human liver type III collagen at 27 degrees C by making a cleavage through the triple helix. The enzyme had no effect on human type I collagen. The reaction was inhibited by phenylmethanesulfonyl fluoride (PhCH2SO2F) but not by EDTA. The collagen reaction products were identical with those generated by human rheumatoid synovial collagenase when analyzed by polyacrylamide gel electrophoresis and gel filtration. NH2-trminal sequence analysis indicated that the enzyme cleaved at an isoleucyl-threonyl bond located 4 residues on the carboxyl side of the established cleavage site for animal collagenases. Therefore, it is likely that in pathologic states, type III collagen can be selectively depleted from the matrix by this enzyme.
纯化的多形核白细胞弹性蛋白酶在27℃通过切割三股螺旋降解天然人肝III型胶原。该酶对人I型胶原无作用。反应受苯甲磺酰氟（PhCH2SO2F）抑制，但不受EDTA抑制。通过聚丙烯酰胺凝胶电泳和凝胶过滤分析，胶原反应产物与人类风湿性滑膜胶原酶产生的产物相同。氨基末端序列分析表明，该酶在位于动物胶原酶既定切割位点羧基侧4个残基处的异亮氨酰-苏氨酰键处切割。因此，在病理状态下，III型胶原很可能可被该酶从基质中选择性地消耗。
