Potempa J, Korzus E, Dubin A, Silberring J
Folia Histochem Cytobiol. 1986;24(2):149-56.
Three proteinases from the azurophilic granules of horse leucocytes are typical elastases degrading elastin at neutral pH. Both proteinases: 1 and 2A exhibit similar elastinolytic activity, comparable with human leucocyte elastase (HLE). In relation to human enzyme, elastase 2B shows several-fold higher activity, which is comparable to the porcine pancreatic elastase activity (PPE). Similarly to HLE elastinolytic activity of the horse proteinases increases at higher ionic strength: twofold in case of 1 or 2A and fivefold for 2B. Significant activity observed during degradation of homologous lung elastin, implies the possible role of these enzymes during pathological injury of connective tissue in the lower respiratory tract and suggests similar pathogenesis of horse and human pulmonary emphysema.
来自马白细胞嗜天青颗粒的三种蛋白酶是典型的弹性蛋白酶,可在中性pH值下降解弹性蛋白。蛋白酶1和2A均表现出相似的弹性蛋白分解活性,与人类白细胞弹性蛋白酶(HLE)相当。与人类酶相比,弹性蛋白酶2B的活性高出几倍,与猪胰弹性蛋白酶活性(PPE)相当。与HLE类似,马蛋白酶的弹性蛋白分解活性在较高离子强度下会增加:蛋白酶1或2A增加两倍,蛋白酶2B增加五倍。在同源肺弹性蛋白降解过程中观察到显著活性,这意味着这些酶在 lower respiratory tract 结缔组织的病理损伤过程中可能发挥作用,并提示马和人类肺气肿的发病机制相似。