Alkaline phosphatase from Echinococcus multilocularis: purification and characterization

• Published in: Comparative biochemistry and physiology. B, Comparative biochemistry Vol. 100; no. 2; pp. 253 - 258
• Main Authors: Sarciron, M.E., Hamoud, W., Azzar, G., Petavy, A.F.
• Format: Journal Article
• Language: English
• Published: England Elsevier Inc 1991
• Subjects: Alkaline Phosphatase - antagonists & inhibitors; Alkaline Phosphatase - isolation & purification; Alkaline Phosphatase - metabolism; Animals; Chromatography, Affinity; Echinococcus - enzymology; Echinococcus multilocularis; Electrophoresis, Polyacrylamide Gel; Gerbillinae; Hydrogen-Ion Concentration; Isatin - pharmacology; Isoelectric Focusing; Kinetics; Liver - enzymology; Liver - parasitology; Nitrophenols - metabolism; Organophosphorus Compounds - metabolism; Temperature; pNPP; SDS; Tris
• ISSN: 0305-0491
• DOI: 10.1016/0305-0491(91)90370-S

1. 1. Kinetic and physical parameters of purified alkaline phosphatase from Echinococcus multilocularis metacestodes, livers of infected gerbils and control animals were determined. 2. 2. K m values for p- nitrophenyl phosphate was about 0.05 ± 0.02 mM for the three enzymes. 3. 3. V max values were 357 ± 67 nmol/min/mg proteins for metacestode enzyme, and 6.7 ± 1.1 and 6.7 ± 0.8 nmol/min/mg proteins for liver enzyme of infected and control animals, respectively. 4. 4. M r and pI were different for the parasite and hepatic enzyme. 5. 5. The parasite enzyme was less sensitive to the elevation of temperature than hepatic enzyme. 6. 6. The isatin inhibition was a competitive inhibition type for parasite and uncompetitive type for host liver enzyme.