Application of Alkaline Phosphatases from Different Sources in Pharmaceutical and Clinical Analysis for the Determination of Their Cofactors; Zinc and Magnesium Ions

Prospects of using different alkaline phosphatases bearing zinc and magnesium ions in their catalytic and allosteric sites, respectively, in pharmaceutical and clinical analysis were demonstrated. Also their application for the determination of zinc in insulin to control injection quality and magnes...

Full description

Saved in:
Bibliographic Details
Published in:Analytical Sciences 2007, Vol.23(3), pp.357-363
Main Authors: MUGINOVA, Svetlana V., ZHAVORONKOVA, Anna M., POLYAKOV, Alexei E., SHEKHOVTSOVA, Tatyana N.
Format: Article
Language:English
Subjects:
Adsorption
Alkaline Phosphatase - chemistry
Alkaline Phosphatase - metabolism
Coenzymes - analysis
Coenzymes - metabolism
Composite Resins - chemistry
Magnesium - analysis
Magnesium - metabolism
Zinc - analysis
Zinc - metabolism
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:Prospects of using different alkaline phosphatases bearing zinc and magnesium ions in their catalytic and allosteric sites, respectively, in pharmaceutical and clinical analysis were demonstrated. Also their application for the determination of zinc in insulin to control injection quality and magnesium in human urine for the diagnosis and treatment of magnesium deficiency was shown. The reaction of p-nitrophenyl phosphate hydrolysis was chosen as an indicator. The choice of appropriate alkaline phosphatase was substantiated, the influence of the nature of buffer solutions on the behavior of the enzyme-metal systems was studied, and the conditions of the indicator reaction proceeding in the presence of sample matrixes were optimized. Simple, rapid, sensitive, and selective enzymatic procedures for determining zinc and magnesium based on their inhibiting and activating effects on the catalytic activity of alkaline phosphatases from seal and chicken intestine, respectively, were developed.
ISSN:0910-6340
1348-2246
DOI:10.2116/analsci.23.357