We have examined the extracellular phosphatases produced by the terrestrial green alga Chlamydomonas reinhardtii in response to phosphorus deprivation. Phosphorus-deprived cells increase extra-cellular alkaline phosphatase activity 300-fold relative to unstarved cells. The alkaline phosphatases are released into the medium by cell-wall-deficient strains and by wild-type cells after treatment wi...

Alkaline phosphatase from human first trimester placentas was purified, characterized, and compared with alkaline phosphatases from term placenta and liver. Three forms of first trimester placental alkaline phosphatase (I, IIa, and IIb) were isolated; their relative amounts were 35%, 39%, and 26%, respectively. Phosphatases I and IIa were found to be dimers, whereas phosphatase IIb appeared to ...

Alkaline phosphatases [orthophosphoric-monoester phosphohydrolase (alkaline optimum), EC 3.1.3.1] have been examined in liver, bone, kidney, intestine, and placenta from nine mammalian species by quantitative inhibition and thermostability studies and compared with alkaline phosphatases in the corresponding human tissues. In humans, three kinds of alkaline phosphatase can be sharply differentia...

Purification, molecular weights, amino acid compositions, and partial sequencing of intestinal alkaline phosphatases (EC 3.1.3.1) from human adult, human fetal, and bovine sources is reported. Additional sequence information is presented for the bovine liver isozyme. Comparisons are made of the partial primary structures of intestinal alkaline phosphatases with those of the isozymes from liver ...

Alkaline phosphatase is an enzyme commonly expressed in almost all living organisms. In humans and other mammals, determinations of the expression and activity of alkaline phosphatase have frequently been used for cell determination in developmental studies and/or within clinical trials. Alkaline phosphatase also seems to be one of the key markers in the identification of pluripotent embryonic ...

1. Purified alkaline phosphatases from cow's milk and calf intestinal mucosa quantitatively convert TPN into DPN. DPN is not hydrolysed by either enzyme. 2. These results confirn that the third phosphate grouping of TPN is esterified (to ribose), since the action of both purified phosphatases is restricted to phospho mono-esters and amides. 3. Under the experimental conditions used, there was n...