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Biomedical subjects

Y M Heimer

Publications and source records attributed to Y M Heimer.

28 records · Page 2Linked to original sources
PubMed1979

Posttranscriptional control of nitrate reductase of cultured tobacco cells by amino acids.

Using the inhibitor of RNA synthesis, 4,5',8-trimethylpsoralen plus near ultraviolet light, the half-life of the rate-limiting RNA species required for the induction of nitrate reductase in XD cells of tobacco was estimated to be 4 hours. Amino acids, the end product of nitrate assimilation, reduced the half-life to 1 hour. It is suggested that amino acids exert a posttranscriptional control on the enzyme level.

Journal Article↗
PubMed1978

Photosensitized inhibition of nitrate reductase induction by 4,5',8-trimethylpsoralen and near ultraviolet light.

4,5' ,8-trimethylpsoralen photosensitizes the inhibition of the induction of nitrate reductase in XD cells of tobacco, by near ultraviolet light. The photosensitization depends on the concentration of 4,5' ,8-trimethylpsoralen and the near ultraviolet light dose. Concomitant with the inhibition of nitrate reductase induction there is a severe inhibition of DNA and RNA synthesis. Oxygen uptake and protein synthesis are not affected. Translation of preexisting mRNA coding for nitrate reductase is insesitive to 4,5' ,8-trimethylpsoralen and near ultraviolet light. It is concluded that the DNA of these cells is the target for the photochemical reaction of 4,5' ,8-trimethylpsoralen. The template activity of the DNA is inhibited, and the expression of the genome thereby prevented. Translation of preexisting nRNA is not affected.

Coumarins↗
PubMed1976

Specificity for Nicotinamide Adenine Dinucleotide and Nicotinamide Adenine Dinucleotide Phosphate of Nitrate Reductase from the Salt-tolerant Alga Dunaliella parva.

Nitrate reductase of the salt-tolerant alga Dunaliella parva could utilize NADPH as well as NADH as an electron donor. The two pyridine nucleotide-dependent activities could not be separated by either ion exchange chromatography on DEAE-cellulose or gel filtration on Sepharose 4B. The NADPH-dependent activity was not inhibited by phosphatase inhibitors. NADPH was not hydrolyzed to NADH and inorganic phosphate in the course of nitrate reduction. Reduction of nitrate in vitro could be coupled to a NADPH-regenerating system of glycerol and NADP-dependent glycerol dehydrogenase. It is concluded that the nitrate reductase of D. parva will function with NADPH as well as NADH. This is a unique characteristic not common to most algae.

Journal Article↗
PubMed1975

Nitrate reductase of Dunaliella parva: electron donor specificity and heat activation.

Nitrate reductase of the salt tolerant alga Dunaliella parva, in contrast to that of most green algae, can use NADPH as well as NADH as electron donor. Extracts of cells contained various amounts of latent nitrate reductase. The latent enzyme could be activated at 45 degrees C but only in the presence of flavine adenine dinucleotide. The heat activated enzyme did not require flavine adenine dinucleotide for activity and was fully active with NADH, NADPH or reduced flavine mononucleotide as electron donors.

Chlorophyta↗