Properties of renal aldosterone-binding proteins.
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Aldosterone↗
Biomedical subjects
J F Wheldrake
Publications and source records attributed to J F Wheldrake.
Structural requirements of inhibition of polyphenylalanine synthesis by aminoacyl and nucleotidyl analogues of puromycin.
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Amino Acids↗
The oxidation of cyst(e)ine by mast-cell tumour P815 in culture.
1. Mast-cell tumour P815 cells oxidize [(35)S]cyst(e)ine to (35)SO(4) (2-). 2. Addition of cysteinesulphinate or sulphite decreases the formation of (35)SO(4) (2-); at the same time [(35)S]cysteinesulphinate or (35)SO(3) (2-) accumulates. 3. Extracts of P815 cells form sulphite from cysteinesulphinate and 2-oxoglutarate. The K(m) for cysteinesulphinate is 6.35mm and that for 2-oxoglutarate is 0.165mm. 4. Extracts oxidize sulphite to sulphate. 5. No formation of hydrogen sulphide from cyst(e)ine was detectable. 6. It is concluded that P815 cells oxidize cyst(e)ine to sulphate solely via cysteinesulphinate and sulphite. 7. The concentration of the enzymes catalysing this sequence is unaltered by several variations in the conditions of growth.
Animals↗
The control of sulphate reduction in Escherichia coli by O-acetyl-L-serine.
1. Extracts of Escherichia coli A.T.C.C. 9723 and K(12)703 contain serine transacetylase and O-acetylserine sulphhydrase. Synthesis of the latter enzyme is repressed by growth on l-cyst(e)ine and other sulphur compounds. 2. O-Acetyl-l-serine added to cells growing on glutathione or sulphate as source of sulphur induces the enzymes that catalyse (a) the activation of sulphate to adenosine 3'-phosphate 5'-sulphatophosphate (EC 2.7.7.4 and 2.7.1.25), (b) the reduction of adenosine 3'-phosphate 5'-sulphatophosphate to sulphite and (c) the reduction of sulphite to sulphide (EC 1.8.1.2). Hydrogen sulphide is liberated from cultures growing on sulphate as source of sulphur and in the presence of O-acetylserine. 3. The cysE mutants of E. coli K(12) lack serine transacetylase. Addition of O-acetylserine permits growth on sulphate as source of sulphur; at the same time the enzymes of sulphate reduction, previously absent, are synthesized. Such mutants have no detectable intracellular cyst(e)ine when starved of sulphur. 4. These results suggest that O-acetylserine is necessary for synthesizing the enzymes of sulphate reduction in E. coli. Its action does not appear to be by interference with the repressive control exerted over these enzymes by cyst(e)ine.
Acyltransferases↗
Intracellular concentration of cysteine in Escherichia coli and its relation to repression of the sulphate-activating enzymes.
1. The intracellular cysteine and glutathione concentrations were measured in Escherichia coli under a variety of growth conditions. 2. An inverse relation between intracellular cysteine concentration and the specific activity of the sulphate-activating enzymes was found. 3. This is compatible with the view that the intracellular cysteine concentration controls the rate of synthesis of these enzymes.
Adenine Nucleotides↗