Resolution, specificity and transphosphorylase activity of calcifying cartilage alkaline phosphatases.

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.