Topping R M, Seilman S
Biochem J. 1979 Feb 1;177(2):493-9. doi: 10.1042/bj1770493.
Kinetic evaluation of the capacity of human blood serum to form complexes with bovine trypsin generated partition profiles that may be approximated by a series of four intersecting straight lines. Such profiles are suggested to reflect the binding of trypsin to alpha 2-macroglobulin in a kinetically preferred mode (alpha-sites), followed by a subsidiary mode (beta-sites) and finally to alpha 1-antitrypsin. The form of the profile, in addition to revealing a hitherto unreported proteinase-binding capability of alpha 2-macroglobulin (beta-sites), also indicates that saturation of alpha-sites corresponds to a molar binding ratio of alpha 2-macroglobulin/trypsin of 1:2. Finally the profile provides, for certain pathological states, a clinically valuable characteristic.
对人血清与牛胰蛋白酶形成复合物能力的动力学评估产生了分配曲线,这些曲线可用一系列四条相交直线近似表示。这种曲线被认为反映了胰蛋白酶以动力学上优先的模式(α位点)与α2-巨球蛋白结合,随后是次要模式(β位点),最后与α1-抗胰蛋白酶结合。该曲线的形式,除了揭示α2-巨球蛋白迄今未报道的蛋白酶结合能力(β位点)外,还表明α位点的饱和对应于α2-巨球蛋白/胰蛋白酶的摩尔结合比为1:2。最后,该曲线为某些病理状态提供了具有临床价值的特征。