Guanidinium-induced differential kinetic denaturation of alkaline phosphatase isozymes.
This paper examines the solution kinetics of bovine intestinal and liver alkaline phosphatase (ALP) isozymes. 4-Methylumbelliferyl phosphate is used as the substrate to study the differential kinetic behavior of ALP isozymes in the presence of guanidinium hydrochloride, a denaturant. The recursive Kalman filter algorithm for parameter estimation is used for analysis of the resulting kinetic data. A two-component first-order kinetic model with a zero-order component is used to successfully quantify intestinal and liver isozymes in synthetic mixtures. This work serves as a basis for the development of an electrophoresis separation method for ALP isozyme quantification with differential kinetic detection.
Lewis
W H
WH
Department of Chemistry, Virginia Commonwealth University, Richmond 23284.
Rutan
S C
SC
D000469:Alkaline Phosphatase / Q000737:chemistry*; D000818:Animals; D002417:Cattle; D019791:Guanidine; D006146:Guanidines / Q000737:chemistry*; D007422:Intestines / Q000201:enzymology; D007527:Isoenzymes / Q000737:chemistry*; D007700:Kinetics; D008099:Liver / Q000201:enzymology; D011489:Protein Denaturation
D006146:Guanidines; D007527:Isoenzymes; D000469:Alkaline Phosphatase; D019791:Guanidine