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M Levinthal

Publications and source records attributed to M Levinthal.

29 records · Page 2Linked to original sources
PubMed1972

The pi-histidine factor of Salmonella typhimurium: a demonstration that pi-histidine factor integrates into the chromosome.

The Salmonella typhimurium pi-histidine episome was identified by Ames et al. (2) in an unstable partial revertant of a deletion mutation-containing strain, hisG203. HisG203 lacks the histidine operator, promoter, and part of the first structural gene. In this paper, we study some properties of pi factor and demonstrate a low frequency of pi integration into the chromosome at or near the histidine region.

Acridines↗
PubMed1971

Biochemical studies of melibiose metabolism in wild type and mel mutant strains of Salmonella typhimurium.

I identified two enzyme activities, alpha-galactosidase and a galactoside permease, required for melibiose metabolism by Salmonella typhimurium. These activities are very low under normal growth conditions, but their production can be induced by melibiose and gratuitously by melibiitol. Melibiose induction is severely inhibited by glucose, but the glucose effect can be countered by 3', 5' cyclic adenosine monophosphate. I isolated two phenotypic classes of mutants not able to utilize melibiose as a carbon source. One class, Car(-), is deficient in the phosphotransferase system. The other, Mel, lacks either alpha-galactosidase, galactoside permease, or both functions.

Adenine Nucleotides↗
PubMed1969

Biosynthesis of cell wall lipopolysaccharide in mutants of Salmonella. V. A mutant of Salmonella typhimurium defective in the synthesis of cytidine diphosphoabequose.

A mutant of Salmonella typhimurium LT2 was found to be unable to convert cytidine diphospho-4-keto-6-deoxy-d-glucose into cytidine diphosphoabequose. The mutation maps in the rfb gene cluster, which is known to be involved in the biosynthesis of the peripheral, "O side-chain" portion of cell wall lipopolysaccharide. In spite of the fact that, in the O side chains, abequose is not a part of the main chain but occurs as short branches, the mutant appears to be unable to polymerize oligosaccharide "repeat units" into long O side chains. The following evidence indicates that this failure is the result of the absence of cytidine diphosphoabequose rather than that of a superimposed second mutation in other genes of the rfb cluster. (i) The mutant does not behave like a multisite mutant in genetic crosses, and it gives rise, at a high frequency, to "revertants" where the ability to synthesize cytidine diphosphoabequose and the ability to synthesize normal lipopolysaccharide with O side chains are both restored. (ii) The mutant strain has normal levels of activity of all of the other enzymes known to be involved in O side-chain synthesis, except that the levels of several enzymes were lowered by about 30% owing to the polarity effect of the mutation. That the lowering of these enzymes is not responsible for the failure of the mutant to synthesize O side chains is clear from the fact that there were revertants which had regained some ability to synthesize abequose but still had lowered levels of these other enzymes, and that this type of revertant produced lipopolysaccharide with considerable amounts of O side chains.

Carbohydrates↗
PubMed1969

Genetic analysis of carbohydrate transport-deficient mutants of Salmonella typhimurium.

Mutants (car) isolated from Salmonella typhimurium were unable to utilize or ferment the following carbohydrates (all d-configuration): glucose, fructose, mannose, N-acetylglucosamine, sorbitol, mannitol, maltose, melibiose, and glycerol. The mutants did utilize galactose, glucose 6-phosphate, gluconic acid, glucuronic acid, pyruvate, and l-lactate. Biochemical analysis showed that there were two classes of mutants, each lacking one component of a phosphotransferase system. CarA mutants were deficient in enzyme I; carB lacked the phosphate carrier protein, HPr. Mapping experiments showed that the carA gene was located near pro; the carB gene mapped near purC.

Biological Transport↗
PubMed1968

Studies of sulfate utilization by algae. 4. Properties of a cell-free sulfate-reducing system from chlorella.

A cell-free system from Chlorella pyrenoidosa Chick (Emerson strain 3) which produces acid-volatile radioactivity from (35)SO(4) (2-) is described. A high speed supernatant from cells broken in the French Press at pH 7.0 shows maximal activity when fortified with ATP, an ATP-generating system (creatine phosphate and creatine phosphokinase), TPN, a TPN-reducing system (glucose-6-phosphate and glucose-6-phosphate dehydrogenase) and MgCl(2). This system is quite labile and is not stable to dialysis. Addition of low concentrations of 2,3,-dimercaptopropan-1-ol (BAL) to the buffers used for enzyme preparation stabilize the extracts and permit them to be dialyzed for 4 hours without loss of activity. If additional BAL is also added to the incubation mixtures it can replace TPNH as a reductant. DPNH also shows appreciable acticity.The system prepared with BAL-containing buffers shows maximal activity at pH 9.0. At this pH, the system requires only ATP, Mg(2+) and additional BAL and has high activity and stability compared with the other conditions tried. The optimum concentrations of these reactants has been determined and the kinetics of production of acid-volatile radioactivity are described. Nucleoside triphosphates other than ATP are not appreciably active in this system. In all cases, anaerobic conditions are required for maximal activity, the enzyme extracts are labile to heat, and no unequivocal requirement for thioctic acid can be demonstrated.

Journal Article↗
PubMed1968

Studies of sulfate utilization by algae. 5. Identification of thiosulfate as a major Acid-volatile product formed by a cell-free sulfate-reducing system from chlorella.

Separation of the products formed from sulfate-(35)S by cell-free extracts of Chlorella pyrenoidosa (Emerson Strain 3) has permitted the identification of thiosulfate as a major product which yields acid-volatile radioactivity. The products formed, as separated by Dowex-1-nitrate chromatography, are qualitatively the same whether extracts at pH 7.0 (using TPNH as the reductant) or extracts at pH 9 [using 2,3-dimercaptopropan-1-ol, (BAL) as reductant] are employed. While thiosulfate can be separated without the addition of carrier, the inclusion of carrier improves the recovery. High concentrations of ATP which have been shown previously to inhibit the formation of acid-volatile radioactivity from radioactive sulfate, inhibit the formation of thiosulfate almost completely. Degradation of the thiosulfate formed at normal ATP concentrations reveals that most of the radioactivity is in the SO(3)-sulfur of the molecule suggesting that the SH-sulfur is derived from the enzyme extracts. If carrier sulfite is present during thiosulfate formation from sulfate-(35)S, radioactive sulfite is recovered at the expense of radioactive thiosulfate. Reconstruction experiments utilizing specifically-labeled thiosulfates indicate that radioactive sulfite formation is probably not the result of trapping a normal intermediate, but can be attributed to non-enzymatic exchange between labeled thiosulfate formed from sulfate and the non-radioactive sulfite added, suggesting that free sulfite is not an intermediate in thiosulfate formation from sulfate.

Journal Article↗
PubMed1968

Studies of Sulfate Utilization by Algae. 6. Adenosine-3'-Phosphate-5'-Phosphosulfate (PAPS) as an Intermediate in Thiosulfate Formation From Sulfate by Cell-Free Extracts of Chlorella.

When cell-free preparations of Chlorella pyrenoidosa Chick (Emerson strain 3) form thiosulfate from labeled sulfate, another radioactive compound also appears. This compound has been isolated in quantity and is shown to be identical with adenosine-3'-phosphate-5'-phosphosulfate (PAPS) on the basis of its chromatographic and electrophoretic behavior, chemical composition, sensitivity to selective degradative enzymes, and its ability to serve as a substrate for rat liver aryl sulphotransferase. In addition, as expected for PAPS, the compound on mild acid treatment yields all of its radioactive sulfur as sulfate, and is converted to a compound identical with adenosine-3',5'-diphosphate (PAP). Replacement of sulfate and ATP by this PAP(35)S in the usual incubation mixture yields the same product, thiosulfate, which can be isolated as such or detected as acid-volatile radioactivity. This conversion of PAP(35)S to thiosulfate still requires the addition of Mg(2+) and a reductant such as 2,3-dimercaptopropan-1-ol (BAL). The cause of our previous result that high concentrations of ATP inhibit thiosulfate formation from sulfate can be ascribed to a small amount of PAP contaminating the ATP preparations, since PAP proves to be an exceedingly effective inhibitor of the conversion of PAP(35)S to thiosulfate. Sulfate reduction to thiosulfate by Chlorella extracts is discussed and compared with similar systems from other organisms.

Journal Article↗