草鱼α2巨球蛋白的分离纯化与若干特性-CURRENTZOOLOGY.PDF

动物学报 　50 (2) :308 - 312 , 2004 A cta Zoologica S inica 　　　　　 　 草鱼 α 巨球蛋白的分离纯化与若干特性 2 李凤玲　陆承平 南京农业大学动物医学院 , 南京 210095 Purif ication and characterization of αmacroglobulin from grass carp Ctenopharyn 2 godon idellus L I FengLing , L U ChengPing College of Veterinary Medicine , Nanjin g Agricultural University , Nanjin g 　210095 , China α ( ) Abstract 　 2Macroglobulin was purified from grass carp plasma by precipitation with polyethylene glycol PEG 6000 , gel filtration and anionexchange chromatography. The three steps of the procedure resulted in the purification of grass carp plasma αM. The purified product was analyzed by polyacrylamide gel electrophoresis ( PA GE) under natural condi 2 tions and the proteins showed a single band. Meanwhile , it was analyzed by SDSPA GE under reducing conditions and the proteins showed double bands with molecular weight of about 95 kD and 80 kD. This result demonstrated that grass carp αM was composed of two distinct subunits. Most properties of grass carp αM were similar to that of human αM. Grass 2 2 2 carp αM treated with trypsin produced the fastform of the molecule more mobile in PA GE , but the untreated grass carp 2 αM had the propert y of electrophoretically slowform. αM was a nonspecific proteinase inhibitors of blood plasma. Inhi 2 2 bition of activity of Aeromonase hydrophilas extracellular proteinase (AhECPase) showed that grass carp αM could