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《Chinese Journal of Animal and Veterinary Sciences》 2004-01
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Isolation,Purification and Properties of Alkaline Phosphatase from Sperm of PIC Pigs(PIC344)

GUO Jin-lin~1,LIU Ke-wu~1,YUE Bi-song~1,ZHANG Zhi-he~1,HOU Rong~1,LI Jia~1,TAO Ke~1,HUANG Yue-wu~2(1.College of Life Science,Sichuan University,Chengdu 610064;2.Pig Breeding Factory of Jingyan,Sichuan)  
Alkaline phosphatase(AKP) was isolated and purified from the sperm of PIC pigs(PIC344) and its kinetic property was examined.The partially purified AKP was purified by salting-out,DEAE-Sepharose FF ion-exchange column,and gel filtrition with sephacryl S-200.The purified enzyme moved as a single electrophoretic band in PAGE.The specific activity was 81.23U/mg.It's subunit weight was 48.41 KD with SDS-PAGE,moleculer weight was 90.12 KD with gel filtrition on Sephacryl S-300(AKTA FPLC).The optimun pH value for the enzyme was 9.5.The optimun temperature for the enzyme was about 40℃.The Michealis-Menton constant(Km) was 3.98×10~(-4)mol/L with disodium phenyl phosphate as its substrate.Ni~(2+),Ca~(2+),Mg~(2+),Sn~(2+) could activate the enzyme determined from 1 mmol/L to 8 mmol/L,Cu~(2+),Cd~(2+) could inhibit the enzyme from 1mmol/L to 3 mmol/L.CuSO_4,Cd(NO_3)_2 was selected for determing types of inhibition,and the result showed that CuSO_4 was a noncompetitive inhibitor,the inhibition constant being 1.32×10~(-3)mol/L,Cd(NO_3)_2 was a competitive inhibitor,with inhibition constant 3.33×10~(-4)mol/L.
【CateGory Index】: S852.2
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