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Biomedical subjects

A C Wilson

Publications and source records attributed to A C Wilson.

At least 253 records · Page 14Linked to original sources
PubMed1972

Enzyme evolution in the Enterobacteriaceae.

An immunological approach has been used for the study of alkaline phosphatase evolution in bacteria of the family Enterobacteriaceae. Antisera were prepared against alkaline phosphatase from Escherichia coli and Klebsiella aerogenes and tested against the unpurified alkaline phosphatases of 32 strains of enterobacteria by double diffusion and quantitative micro-complement fixation. The immunological relationships detected among the alkaline phosphatases of enterobacteria agree approximately with those reported for five other enzymes, as well as with the tryptic peptide pattern similarities found for two other enzymes, and with the relationships detected by interspecific deoxyribonucleic acid hybridization tests.

Alkaline Phosphatase↗
PubMed1972

Micro-complement fixation in Klebsiella classification.

The alkaline phosphatases of 29 strains of bacteria assigned by various authors to the genera Aerobacter, Klebsiella and Enterobacter were compared by the micro-complement fixation technique. On the basis of phosphatase resemblance, we recommend that all strains hitherto assigned to Aerobacter aerogenes and Enterobacter aerogenes be assigned to the genus Klebsiella.

Alkaline Phosphatase↗
PubMed1971

Albumin evolution in frogs: a test of the evolutionary clock hypothesis.

Frogs are an ancient group compared to placental mammals. Yet, although there are about as many species of frogs as there are of mammals, zoologists consider that frogs have undergone only limited morphological divergence, while placental mammals have diversified greatly in morphology and way of life. The serum albumins of numerous frog species were compared by the quantitative microcomplement fixation technique. Frogs that are morphologically similar enough to merit taxonomic distinction at only the species level often exhibit differences in the serological properties of their albumins larger than those usually seen between mammals placed in distinct families or suborders. Thus, there seems to be a contrast between albumin evolution and evolution at the organismal level. The large differences between albumins among frogs can be explained by the hypothesis that albumin evolution has proceeded at the same rate in frogs as in mammals.

Acrylamides↗
PubMed1970

Comparative immunological studies of two Pseudomonas enzymes.

Crystalline preparations of muconate lactonizing enzyme and muconolactone isomerase, two inducible enzymes that catalyze successive steps in the catechol branch of the beta-ketoadipate pathway, were used to prepare antisera. Both enzymes were isolated from a strain of Pseudomonas putida biotype A. The antisera did not cross-react with enzymes of the same bacterial strain that catalyze the chemically analogous steps in the protocatechuate branch of the beta-ketoadipate pathway, carboxymuconate lactonizing enzyme and carboxymuconolactone decarboxylase. The antisera gave heterologous cross-reactions of varying intensities with the muconate lactonizing enzymes and muconolactone isomerases of P. putida biotype B, P. aeruginosa, P. stutzeri, and all biotypes of P. fluorescens, but did not cross-react with the isofunctional enzymes of P. acidovorans, of P. multivorans, and of two bacterial species that belong to other genera. The evolutionary and taxonomic implications of the findings are discussed.

Animals↗
PubMed1969

Immunological detection of single amino acid substitutions in alkaline phosphatase.

Antiserums to wild-type alkaline phosphatase from Escherichia coli were prepared and tested for reactivity with phosphatases altered by point mutations. Eight out of the nine mutant enzymes were distinguished from the wild type with quantitative microcomplement fixation. The structural changes are among the smallest yet observed immunologically.

Alkaline Phosphatase↗