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Citrate and the conversion of carbohydrate into fat. A comparison of citrate and acetate incorporation into fatty acids.
culture medium. It is now realized that arylsulphatase can be produced in the absence of tyramine if a non-repressor sulphur compound is used as the sulphur source, and that the enzyme can also beExpand
Purification and kinetic characteristics of dogfish liver glutamate dehydrogenase.
TLDR
The molecular weight of the enzyme has been determined and the sedimentation constant has been found to be invariant over a wide range of concentrations, in contrast to the bovine liver glutamate dehydrogenase. Expand
Kinetic studies of dogfish liver glutamate dehydrogenase with diphosphopyridine nucleotide and the effect of added salts.
TLDR
Kinetic studies have been performed with crystalline dogfish liver glutamate dehydrogenase with the diphosphopyridine nucleotides as cofactors, and added salt minimized the regulatory influence of the nucleotide guanosine 5'-triphosphate and adenosine 5-diphosphate. Expand
Alterations in Dihydropteroate Synthetase in Cell-Free Extracts of Sulfanilamide-Resistant Neisseria meningitidis and Neisseria gonorrhoeae
TLDR
A direct relationship was observed between the minimal inhibitory concentration of sulfanilamide determined in vitro and the ratio of Ki/Km, which may be a molecular explanation of sulfAnilamide resistance for both N. meningitidis and N. gonorrhoeae. Expand
[118] l-Glutamate dehydrogenase (dogfish liver and chicken liver)
TLDR
This chapter discusses the assay, purification, and properties of L-glutamate dehydrogenase, an enzyme isolated from the liver of the dogfish that has the virtue of being relatively stable under most conditions and is not subject to the reversible association–dissociation reaction characteristic of other glutamate dehydrogenases. Expand
Structure-Activity of Sulfones and Sulfonamides on Dihydropteroate Synthetase from Neisseria meningitidis
TLDR
The molecular interaction of various sulfones and sulfonamides with partially purified dihydropteroate synthetase from Neisseria meningitidis M-166 has been examined and 4,4′-Diaminodiphenylsulfone was three times more effective than sulfadiazine and nine times moreeffective than sulfanilamide as a competitive inhibitor of dihydopteroatesynthetase. Expand
A simple radioassay for dihydrofolate synthetase activity in Escherichia coli and its application to an inhibition study of new pteroate analogs.
TLDR
A simple, rapid, and accurate radioassay method, using L-[ 14 C]glutamic acid as substrate, is developed for a quantitative determination of dihydrofolate synthetase activity in Escherichia coli. Expand
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