Apr 20, 1976

Resolution, specificity and transphosphorylase activity of calcifying cartilage alkaline phosphatases

Calcified Tissue Research
C ArsenisS M Huang

Abstract

The phosphate releasing activity from calf scapula cartilage was resolved by DEAE-cellulose chromatography into two distinct phosphatase activities. The activity eluted first from the column (phosphatase I) was active towards a variety of phosphate esters and several linear oligo phosphates including sodium pyrophosphate, while the second phosphatase activity (phosphatase II) was active only towards simple phosphate esters. Phosphatase I acted towards oligo phosphates in a stepwise fashion hydrolyzing one phosphate at a time. Both phosphatase are sialoproteins and can transfer phosphate from any of their substrates into other than water phosphate acceptor molecules such as glycerol. By several criteria, it can be concluded that the two phosphatases are different enzyme entities.

Mentioned in this Paper

Cations, Divalent
Alkaline Phosphatase
Sialic Acids
Phosphotransferases
Diphosphates
Bos indicus
Orthophosphate
Adenine Nucleotides
Cartilage
Hydrogen-Ion Concentration

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