Near-ultraviolet radiation was found to be lethal for mammalian cells in Dulbecco's modified Eagle's medium without serum or phenol red. Irradiation of the cells with near-ultraviolet light while the cells were in phosphate-buffered-saline abolished the lethal effect. When only the medium was irradiated followed by the addition of unirradiated cells and serum, the cells were still killed. The photoactive components of the medium for this effect were riboflavin, tryptophan, and tyrosine. When riboflavin was deleted from the medium being irradiated and added later, almost no killing was detected. Irradiation of salt solution of riboflavin and tryptophan or riboflavin and tyrosine, resulted in cell killing. Little or no killing resulted when riboflavin, tryptophan, or tyrosine was irradiated singly. The formation of photoproducts toxic for mammalian cells appears to involve photodynamic action. Experiments utilizing Dulbecco's or similar media without proper controls may produce anomalous results from light illuminating the laboratory.

Animals↗

PubMed1971

Effect of pleiotropic carbohydrate mutations (ctr) on tryptophan catabolism.

The pleiotropic ctr mutation has been shown to affect tryptophan uptake and tryptophanase formation. Genetic reversions are of two types: (i) complete, restoring to wild type, located at 46 to 47 min; (ii) partial, restoring only tryptophanase synthesis, located at 73 min. In some strains the effect of ctr mutations could be reversed by cyclic adenosine 3',5'-monophosphate (cAMP) plus tryptophan. A mutant producing tryptophanase constitutively was suppressed by a ctr mutation. Production of tryptophanase in this suppressed strain was not restored by the addition of cAMP, but required cAMP plus tryptophan.

Carbohydrate Metabolism↗

PubMed1970

Carbohydrate Accumulation and Metabolism in Escherichia coli: Characteristics of the Reversions of ctr Mutations.

The reversion behavior of pleiotropic carbohydrate mutants, previously designated as ctr, was studied. The mutants revert to complete restoration of the wild-type phenotype, as well as to a spectrum of partial wild-type phenotypes. Lac(+) reversions were found in the lac region (11 min) and some Mal(+) reversions occurred at malB (79 min), at a distance from the site of the ctr mutations (46 to 47 min). About one-third of Lac(+) and Mal(+) revertants were constitutive for uptake of their respective substrates, and one-third modified for inducibility. The remaining third were not distinguishable from wild type. Induction of a ctr mutation in a lac constitutive strain, either operator or repressor mutant, did not affect lactose metabolism. A polar-like ctr mutant, deficient in both enzyme I and heat-stable protein of the phosphoenolpyruvate-dependent phosphotransferase strain was also described. Partial revertants of ctr were still found to lack enzyme I.

Journal Article↗

PubMed1969

Carbohydrate accumulation and metabolism in Escherichia coli: the close linkage and chromosomal location of ctr mutations.

Six pleiotropic ctr mutations of Escherichia coli, affecting the ability to utilize 10 carbohydrates, were found to be closely linked to one another and to the mutation of strain MM6 causing lack of enzyme 1 of the phosphotransferase system. These mutations are located at 46 to 47 min on the E. coli map. Preliminary biochemical evidence indicates that the ctr mutants also lack enzyme 1, although they have a different phenotype from MM6.

Carbohydrate Metabolism↗

PubMed1968

Carbohydrate accumulation and metabolism in Escherichia coli. I. Description of pleiotropic mutants.

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Arabinose↗