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Functional correlation between the Ser/Thr-phosphorylation of band-3 and band-3-mediated transmembrane anion transport in human erythrocytes.
In human erythrocytes, okadaic acid, a potent inhibitor of certain protein phosphatases, promotes a marked increase of Ser/Thr-phosphorylation of membrane proteins, including band-3 protein.Expand
Partial purification and characterization of phosphotyrosyl-protein phosphatase(s) from human erythrocyte cytosol.
TLDR
Both 32P-Tyr-phosphatase activities distinctly differ from either32P-Ser-casein phosphatase activity or "acid" and "alkaline" p-nitrophenylphosph atase activities with regard to catalytic and physico-chemical properties such as substrate specificity, chromatographic behaviour, response to various effectors. Expand
The Lyn-catalyzed Tyr phosphorylation of the transmembrane band-3 protein of human erythrocytes.
TLDR
It is of interest that Lyn can associate with membranes and markedly phosphorylate band 3 when this latter protein has been previously phosphorylated by p36syk, i.e. the p36(syk)-catalyzed phosphorylation is proposed to be a prerequisite for the association of Lyn with the membrane (likely to band 3) and for the Lyn-catalyzing phosphorylations of different band-3 Tyr sites. Expand
REMOVAL OF THE N-TERMINAL RESIDUE OF A PROTEIN AFTER TRANSAMINATION.
TLDR
Pseudomonas cytochrome c-551 was modified by treatment at 20 degrees with glyoxylate in the presence of pyridine and cupric sulphate to provide a method for specific removal of the N-terminal residue of a protein. Expand
Spermine-mediated casein kinase II-uptake by rat liver mitochondria.
TLDR
Findings suggest that spermine may play a critical role in regulating the subcellular distribution of casein kinase CKII. Expand
Spermine effect on the binding of casein kinase I to the rat liver mitochondrial structures.
The results indicated here, together with those previously reported, show that spermine, ubiquitous polyamine, while promoting the transmembrane translocation of casein kinase II (CKII) across theExpand
Partial purification and characterization of cytosolic Tyr-protein kinase(s) from human erythrocytes.
TLDR
Results suggest that in intact erythrocytes the cytosolic Tyr-protein kinase might phosphorylate band 3 not only on Tyr-8, surrounded by several acidic side-chains, but also on other Tyr residues surrounded by other amino acid sequences. Expand
Phosphorylation of casein fractions by rat liver ‘phosvitin kinase’
TLDR
The aim of this work is to study the phosphorylation of the single casein fractions and determine in which fractions are located the serine and threonine residues involved in the kinase reaction. Expand
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