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Biomedical subjects

J D Kemp

Publications and source records attributed to J D Kemp.

At least 109 records · Page 6Linked to original sources
PubMed1972

Protein Metabolism in Cultured Plant Tissues: III. Changes in the Rate of Protein Synthesis, Accumulation, and Degradation in Cultured Pith Tissue.

During the transition of tobacco (Nicotiana tabacum) pith tissue to callus tissue, there were changes in the composition of the soluble amino acid pools, in the distribution of amino acids between pool and protein, and in the synthesis, accumulation, and degradation of proteins. The size of the leucine pool decreased from 90 nanomoles per gram fresh weight in fresh pith to 20 nanomoles in 24-hour cultured pith, followed by a return to 90 nmoles in pith cultured longer than 5 days. The latter value is the same as that reported for exponentially growing callus cells. Many other pool amino acids changed as dramatically. However, they always approached callus levels after 5 days of culturing. The total amino acid content of pith tissue (the sum of both pool and protein) remained unchanged during culturing. The value for total amino acid content (34 to 42 nanomoles per gram fresh weight) was also similar to that found in callus. The distribution of amino acids between pool and protein did change during culturing. The transition of pith tissue with 88% of its total amino acids free in the soluble pool to callus with 92% of its amino acids in protein was further characterized by changes in protein metabolism. Both protein synthesis and accumulation increased over the first 50 hours in culture to a maximum rate of 45 milligrams protein synthesized gram protein(-1) hour(-1). After 50 hours in culture, the rate of protein accumulation decreased to equal the rate of fresh weight accumulation (10 mg g(-1) hour(-1)). However, protein synthesis continued at a high rate for several days, suggesting protein degradation was turned on by this time. By 5 days protein synthesis had decreased to a rate similar to that of callus.

Journal Article↗
PubMed1970

Gas-Liquid Chromatographic Isolation of Cytokinins from Natural Sources: 6-(3-Methyl-2-butenylamino) purine from Agrobacterium Tumefaciens.

Gas-liquid chromatographic retention times for 20 purines or purine nucleosides, 14 of which are highly active cytokinins, are reported. With one exception, all of the naturally occurring cytokinins are separated.Ethyl acetate extraction of yeast transfer RNA hydrolysates and of culture filtrates of Agrobacterium tumefaciens gave sufficient concentration of the naturally occurring cytokinins for immediate gas-liquid chromatography. This procedure permitted the detection of 6-(3-methyl-2-butenylamino)-9-beta, d-ribofuranosylpurine in yeast transfer RNA extracts. An active cytokinin was isolated from A. tumefaciens culture filtrates and was tentatively identified as 6-(3-methyl-2-butenylamino)purine.

Journal Article↗
PubMed1966

Nitrite reductase of Escherichia coli specific for reduced nicotinamide adenine dinucleotide.

Kemp, John D. (University of California, Los Angeles), and Daniel E. Atkinson. Nitrite reductase of Escherichia coli specific for reduced nicotinamide adenine dinucleotide. J. Bacteriol. 92:628-634. 1966.-A nitrite reductase specific for reduced nicotinamide adenine dinucleotide (NADH(2)) appears to be responsible for in vivo nitrite reduction by Escherichia coli strain Bn. In extracts, the reduction product is ammonium, and the ratio of NADH(2) oxidized to nitrite reduced or to ammonium produced is 3. The Michaelis constant for nitrite is 10 mum. The enzyme is induced by nitrite, and the ability of intact cells to reduce nitrite parallels the level of NADH(2)-specific nitrite reductase activity demonstrable in cell-free preparations. Crude extracts of strain Bn will also reduce hydroxylamine, but not nitrate or sulfite, at the expense of NADH(2). Kinetic observations indicate that hydroxylamine and nitrite may both be reduced at the same active site. The high apparent Michaelis constant for hydroxylamine (1.5 mm), however, seems to exclude hydroxylamine as an intermediate in nitrite reduction. In vitro activity is enhanced by preincubation with nitrite, and decreased by preincubation with NADH(2).

Enzyme Induction↗