Marx G
Coagulation Laboratory, Magen David Adom Blood Services, Tel Hashomer, Israel.
Arch Biochem Biophys. 1988 Oct;266(1):285-8. doi: 10.1016/0003-9861(88)90260-3.
Zinc binding to fibrinogen and fibrin was studied by two techniques. Scatchard analysis of ultrafiltration eluates reveals that fibrinogen has multiple Zn(II)-binding sites, KD (fibrinogen) = 18 microM; n = 6. The zinc content of the "collapsed" fibrin gel supernatant was also determined by atomic absorption spectroscopy and analyzed by a Scatchard plot (KD (fibrin) = 8 microM, n = 6). In other experiments, Zn(II) did not displace 45Ca(II) from fibrin. It appears that the binding of zinc to fibrinogen or fibrin is distinct from that of calcium, and that the zinc-binding characteristics of fibrinogen and fibrin are not significantly affected by the transformation of one into the other.
通过两种技术研究了锌与纤维蛋白原和纤维蛋白的结合。对超滤洗脱液进行Scatchard分析表明,纤维蛋白原有多个Zn(II)结合位点,KD(纤维蛋白原)= 18微摩尔;n = 6。“塌陷”纤维蛋白凝胶上清液中的锌含量也通过原子吸收光谱法测定,并通过Scatchard图进行分析(KD(纤维蛋白)= 8微摩尔,n = 6)。在其他实验中,Zn(II)不会从纤维蛋白中置换出45Ca(II)。看来锌与纤维蛋白原或纤维蛋白的结合不同于钙的结合,并且纤维蛋白原和纤维蛋白的锌结合特性不会因彼此之间的转化而受到显著影响。