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Biomedical subjects

A Oppenheim

Publications and source records attributed to A Oppenheim.

At least 109 records · Page 6Linked to original sources

A pleiotropic regulatory mutation in lambda bacteriophage.

Lambda bacteriophage mutants, lambdasar, were isolated. These mutants can form plaques on a non lysogenic lawn and are unable to grow on nonimmune (imm-), cro constitutive hosts. Analysis of the restriction of lambdasar by a set of defective lysogens suggested that both the cro and cII gene products participate in the inhibition. The sar mutations were mapped in the ori region between the genes cII and O. Complementation experiments showed that under the restrictive conditions lamdasar is defective in the expression of both the N and the O genes. Transcription analyses support these findings, as lambdasar is unable to serve as a template for transcription after infecting cro constitutive hosts. In addition lambdasar does not replicate under the restrictive conditions, although its DNA can bind to the host membrane to some extent. The Sar phenotype can be relieved by removing sites of action of cro either by a V2 mutation or by substituting the lambda immunity region by imm434 or imm21. Similarly introducing a cy mutation, which interferes with the action of the cII gene product, also eliminates the Sar effect. The sar mutation can suppress cy mutations as manifested in plaque morphology, lysogenization frequency, cI repressor synthesis and the expression of rex function. Suppression takes place only when the sar mutation is present in cis to cy and it requires the action of the cII and cIII gene products. It is suggested that the sar mutation suppresses cy by activating a new promoter for repressor synthesis, pro. The results also suggest that the cII and cIII gene products may act at a site other than y.

Chromosome Mapping↗

An acetaldehyde dehydrogenase from germinating seeds.

An acetaldehyde dehydrogenase from germinating peanut cotyledons has been purified and its properties have been studied. At the highest purification achieved the preparation is free of alcohol dehydrogenase activity.The enzyme is specific toward diphosphopyridine nucleotide, and can oxidize a variety of aldehydes. The highest reaction rate is obtained with acetaldehyde, which is oxidized to acetate. All the attempts to demonstrate the formation of an energy-rich acetyl derivative during the course of the reaction failed. The enzyme is inhibited by aldol; it is sensitive toward sulfhydryl reagents, including arsenite. Reduced glutathione stabilizes the enzyme, while cysteine, mercaptoethanol, and coenzyme A are inhibitory.Acetaldehyde dehydrogenase is activated by phosphate and inhibited by fatty acyl-CoA derivatives. It appears to be activated by the substrate, as was deduced from the shape of the plot of reaction velocity against acetaldehyde. These properties suggest that the enzyme is an allosteric protein.The plot of reaction velocity against substrate concentration is anomalous. The shape of this plot seems to reflect the presence of 2 different enzymatic activities, one with extremely high apparent affinity for acetaldehyde. The 2 activities may reflect 2 conformational states of a single enzyme or 2 separate enzymes.Experiments with tissue slices indicate that the reaction catalyzed by this enzyme is a step in the oxidation of ethanol to acetyl-CoA. This enzyme may also participate in the oxidation of pyruvate to acetyl-CoA in certain tissues.

Journal Article↗