Alkaline phosphatase isoenzymes

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Comparison of Human Alkaline Phosphatase Isoenzymes

The structural relationships among human alkaline phosphatase isoenzymes from placenta, bone, kidney, liver and intestine were investigated by using three criteria. 1. Immunochemical characterization by using monospecific antisera prepared against either the placental isoenzyme or the liver isoenzyme distinguishes two antigenic groups: bone, kidney and liver isoenzymes cross-react with anti-(li...

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Plasma alkaline phosphatase isoenzymes in hepatobiliary disease.

BY CELLULOSE ACETATE OR ACRYLAMIDE GEL ELECTROPHORESIS IT IS POSSIBLE TO SEPARATE THESE ALKALINE PHOSPHATASE ISOENZYMES FROM SERUM: [anode] fast liver, slow liver, placenta/Regan, bone, intestine, bile [cathode]. Heat or chemical inhibition can confirm the differentiation. Normal adult serum always contains slow-liver isoenzyme, and sometimes bone isoenzyme: the latter is always present in seru...

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Alkaline phosphatase isoenzymes in plasma in hyperthyroidism.

Alkaline phosphatase (ALP; EC 3.1.3.1) isoenzymes were measured in the plasma of 63 untreated hyperthyroid patients (the hyperthyroid group), 58 treated hyperthyroid patients, and 100 blood donors. Total, liver, and bone ALP activities were significantly higher in the hyperthyroid group than in the treated hyperthyroid group or the blood donors. Bone ALP was more frequently and more markedly ab...

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Serum Alkaline Phosphatase Isoenzymes in Lymphoproliferative Diseases1

A new isoenzyme of alkaline phosphatase (EC 3.1.3.1) has been reported to occur in sera from patients with lymphoproliferative diseases. This enzyme is character ized by an inability to hydrolyze cysteamine S-phosphate. We find that the 5,5 -dithobis(2-nitrobenzoic acid)-coupled assay method for cysteamine S-phosphate hydrolysis is not suitable for serum, and we were unable to confirm the exist...

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Distribution and properties of rat intestinal alkaline phosphatase isoenzymes.

The ALP activities and properties of rat intestine cut into 20 segments were examined, and we were able to demonstrate that the ALP activity of upper intestine is high compared to that of lower intestine. This result coincided with those of other reports. However, we newly clarified that there is an ALP isoenzyme found in the lower intestine which can be inhibited by L-homoarginine. The molecul...

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ژورنال

عنوان ژورنال: SEIBUTSU BUTSURI KAGAKU

سال: 1976

ISSN: 0031-9082,1349-9785

DOI: 10.2198/sbk.20.241