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Biomedical subjects

B D Hall

Publications and source records attributed to B D Hall.

At least 199 records · Page 11Linked to original sources
PubMed1974

Macromolecule synthesis and breakdown in relation to sporulation and meiosis in yeast.

The time course of synthesis and breakdown of various macromolecules has been compared for sporulating (a/alpha) and nonsporulating (a/a and alpha/alpha) yeast cells transferred to potassium acetate sporulation medium. Both types of cells incorporate label into ribonucleic acid and protein. The gel electrophoresis patterns of proteins synthesized in sporulation medium are identical for sporulating and nonsporulating diploids; both are different from electropherograms of vegetative cells. Sporulating and nonsporulating strains differ with respect to deoxyribonucleic acid synthesis; no deoxyribonucleic acid is synthesized in the latter case, whereas the deoxyribonucleic acid complement is doubled in the former. Glycogen breakdown occurs only in sporulating strains. Breakdown of preexisting vegetative ribonucleic acid and protein molecules occurs much more extensively in sporulating than in nonsporulating cells. A timetable of these data is presented.

Adenine↗
PubMed1972

Transcription in yeast: a factor that stimulates yeast RNA polymerases.

Yeast cells contain an RNA polymerase factor, pi, which is a heat-stable protein with an apparent molecular weight of 12,000. This factor stimulates transcription of calf-thymus, salmon-sperm, yeast-nuclear, and T4-phage DNA. It stimulates transcription by each of the four yeast-nuclear RNA polymerases, by rat-liver RNA polymerases I and II, and by Escherichia coli RNA polymerase. pi-Factor can cause each of the eukaryotic RNA polymerases to become insensitive to rifamycin AF-013, but does not stop inhibition of E. coli RNA polymerase by rifamycin AF-013. Stimulation of transcription by pi-factor is general, and does not apply only to a limited class of genes. Apparently, pi-factor stimulates transcription by increasing the proportion of RNA polymerase binding events that leads to the initiation of RNA chains.

Ammonium Sulfate↗
PubMed1972

Transcription in yeast: separation and properties of multiple FNA polymerases.

Four peaks of DNA-directed RNA polymerase activity are resolved by salt gradient elution of a sonicated yeast cell extract on DEAE-Sephadex. The enzymes, which are named IA, IB, II, and III in order of elution, all appear to come from cell nuclei. Only enzyme II is sensitive to alpha-amanitin. All enzymes are more active with Mn(++) than with Mg(++) as divalent ion. Enzymes IB and II have salt optima in the range 0.05-0.10 M (NH(4))(2)SO(4), whereas enzyme III is maximally active at 0.20-0.25 M (NH(4))(2)SO(4). With optimal salt concentration and saturating DNA, the template preference ratio, activity on native calfthymus DNA divided by activity on denatured calf-thymus DNA, is 2.2 for IB, 0.4 for II, and 3.5 for III. None of the yeast polymerases was inhibited by rifamycin SV. Rifamycin AF/013 effectively inhibited polymerases IB, II, and III.

Ammonium Sulfate↗
PubMed1971

Aglossia-adactylia.

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Abnormalities, Multiple↗