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Biomedical subjects

W A Scott

Publications and source records attributed to W A Scott.

At least 163 records · Page 9Linked to original sources
PubMed1973

Rheumatology.

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Adjustment Disorders↗
PubMed1972

Rheumatology.

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Acute Disease↗
PubMed1972

Mechanism of hormonal induction of tyrosine aminotransferase studied by measurement of the concentration of growing enzyme molecules.

Proteins labeled in cultured hepatoma cells grown in the presence of radioactive amino acids and pactamycin consist primarily of growing polypeptide chains initiated before addition of the antibiotic. Nascent tyrosine aminotransferase (EC 2.6.1.5) molecules were labeled in this way, and their radioactivity after completion was measured immunologically. Cells exposed to the synthetic adrenal steroid, dexamethasone, contain 10- to 18- times as much nascent enzyme as uninduced cells. These results indicate that induction control is not at the level of polypeptide-chain elongation or release, but probably operates on either the amount of messenger RNA or the rate of specific polypeptide-chain initiation.

Amino Acids↗
PubMed1970

Glucose-6-phosphate dehydrogenase and Neurospora morphology.

In addition to the Neurospora crassa mutant col-2, mutations in two other unlinked genes, balloon and frost, lead to distinct morphological growth and abnormal glucose-6-phosphate dehydrogenases. The glucose-6-phosphate dehydrogenases from these strains have increased thermolabilities, altered kinetic parameters, and distinctive electrofocusing patterns. The altered enzyme segregates with each morphological phenotype in crosses to wild type, and there is a correlation between the severity of the enzymic defect and the degree of morphological abnormality in heterocaryons and double mutants. These results are compatible with the hypotheses that the balloon, frost, and col-2 genes are structural genes for glucose-6-phosphate dehydrogenase and that the pleiotropic effects of these altered dehydrogenases are responsible for the mutant morphologies.

Genetics, Microbial↗
PubMed1970

Location of Aryl Sulfatase in Conidia and Young Mycelia of Neurospora crassa.

Aryl sulfatase (arylsulfate sulfohydrolase, EC 3.1.6.1) was found to have multiple locations in Neurospora conidia. Some enzyme activity remained in the supernatant when a spore suspension was centrifuged or filtered. Part of the cell-bound activity could be detected by adding the assay ingredients to a suspension of intact spores (patent enzyme), and additional activity was only detectable when the spores were first treated to destroy their permeability barriers (cryptic enzyme). Such treatments include: disruption with an X-press, brief rinsing with chloroform or acetone, incubation at 60 C for 5 min, and incubation with phenethyl alcohol, nystatin, or ascosin. Part of the patent aryl sulfatase was inactivated by briefly acid treating the intact spores (no loss of conidial viability). This enzyme was considered to have a cell surface location. Some enzyme was acid-resistant in intact spores, but all of the enzyme was acid-sensitive in spores whose permeability barriers had been disrupted. The pH dependence, kinetic properties, and p-nitrophenyl sulfate uptake were investigated in acid-treated conidia. No aryl sulfatase was detected in ascospores. Young mycelia contained more aryl sulfatase than did conidia, but little, if any, was secreted into the growth medium. Cryptic activity was demonstrated in young mycelia by brief chloroform treatment or by rinsing the cells with 0.1 m acetate buffer. Enzyme activity in young mycelia was completely labile to acid treatment, as was cell viability.

Journal Article↗