Primary structure of bovine s1 casein. Complete sequence

Dentin phosphoprotein: an extracellular calcium-binding protein.

31P nuclear magnetic resonance (NMR) was used to directly observe the binding of inorganic phosphate to alkaline phosphatase. Evidencq for the tight binding of 1.5-2.0 mol of inorganic phosphate per dimer of alkaline phosphatase is presented. Two distinct forms of bound phosphate are observed, one predominating above pH 7 and representing the non-covalent E-P1 complex and the other predominating below pH 5 and representing the covalent E-P1 complex. The 31P NMR line width of the E-P1 complex indicates that the dissociation of noncovalent phosphate is the rate-limiting step in the turnover of the enzyme at high pH.

Phosphorus-31 nuclear magnetic resonance study of alkaline phosphatase: the role of inorganic phosphate in limiting the enzyme turnover rate at alkaline pH

https://espace.library.uq.edu.au/view/UQ:248987/UQ248987_OA.pdf

Purification and structural characterization of a filamentous, mucin-like proteophosphoglycan secreted by Leishmania parasites

Nuclear magnetic resonance is a new method for assaying the content of phosphate metabolites in intact tissues. Its nondestructive nature allows simultaneous and repeated determinations of these compounds with a minimum perturbation of tissue. Changes in the concentrations of the phosphates as a function of time characterize the metabolic machinery of the tissue and reveal alterations in enzymic activity that result from drug treatment or disease. The entire phosphate profile shows differences between normal and diseased muscle which should be of diagnostic value. Further, by examining phosphate profiles we detected a family of chemical compounds that were not previously known to exist as major constituents in muscle. Of these, two have been isolated and one has been identified as glycerol 3-phosphorylcholine. Finally, shifts in the positions of resonances monitor the internal environment of the living system, its hydrogen ion concentration, the complexing of alkaline earth metals with ATP, and compartmentalization within the cell.

Analysis of living tissue by phosphorus-31 magnetic resonance.

Phosphorus nuclear magnetic resonance studies of phosphoproteins and phosphorylated molecules. II. Chemical nature of phosphorus atoms in alpha S-casein B and phosvitin.

Robert J. Kurland

Papers

Phosphorus nuclear magnetic resonance studies of phosphoproteins and phosphorylated molecules. II. Chemical nature of phosphorus atoms in alpha S-casein B and phosvitin.