Veronese F M, Largajolli R, Schiavon O, Casati P
Farmaco Sci. 1987 May;42(5):319-23.
A very high molecular weight form of urokinase, of about 100,000 D (VHMr-UK), was isolated from human urine in trace amounts as compared to the well characterized two forms of urokinase, HMr-UK (Mr of about 50,000) and LMr-UK (Mr of about 30,000). This form was demonstrated to be a dimer of HMr-UK, in which no covalent bond is involved, on the basis of the following evidence: by SDS electrophoresis it is dissociated, to the 50,000 D form; by electrophoresis in SDS under reducing conditions it is dissociated, as HMr-UK, to two polypeptide chains of about 30,000 and 20,000 D; by short heating at pH 5 it is quantitatively converted to the 50,000 D form; the kinetic constants towards the alpha-carbobenzoxy-L-lysine-p-nitro-phenylester substrate are the same for HMr-UK and VHMr-UK.
与已充分表征的两种尿激酶形式,即重链尿激酶(HMr-UK,分子量约50,000)和轻链尿激酶(LMr-UK,分子量约30,000)相比,一种分子量非常高的尿激酶形式,约100,000 D(VHMr-UK),仅从人尿中微量分离得到。基于以下证据表明,这种形式是HMr-UK的二聚体,其中不涉及共价键:通过SDS电泳,它解离为50,000 D的形式;在还原条件下进行SDS电泳时,它像HMr-UK一样解离为两条分别约为30,000和20,000 D的多肽链;在pH 5下短暂加热,它定量转化为50,000 D的形式;HMr-UK和VHMr-UK对α-苄氧羰基-L-赖氨酸-对硝基苯酯底物的动力学常数相同。