Biomedical subjects

K P Mitton

Publications and source records attributed to K P Mitton.

21 records · Page 2Linked to original sources

PubMed1989

Acetate assimilation by the fission yeast, Schizosaccharomyces pombe.

The fission yeast Schizosaccharomyces pombe utilizes acetate at subinhibitory concentrations in the presence of D-glucose. The nonionized form of acetate is preferentially utilized, oxidized to 14CO2, and assimilated into lipids and proteins. Acetyl CoA synthetase activity greatly increases in the yeast cells grown in media containing acetate. However, glyoxylate cycle enzymes are not detectable in Schizosaccharomyces pombe. [1-14C]Acetate is incorporated into stereols, sterol esters, neutral lipids, and phospholipids. Assimilation of [1-14C]acetate into the peptide structure of proteins was confirmed by a proteolytic digestion experiment.

Acetates↗

PubMed1989

Modelling cortical cataractogenesis. X. Evaluation of lens optical function by computer based image analysis using in vitro rat lens elevated glucose model.

As a model system rat lenses (Wistar) were isolated and cultured intact in medium M199 or M199 with 55 mM glucose. Glucose-stressed lenses developed opacities within 20 hours while control lenses remained clear. The comparative functionality of lenses was examined by two different video/computer-based imaging systems: one based on image analyses of laser light after transmission through the lens (Scanning Lens Monitor), and the other based on image analyses of the projection of white light transmitted through the lens (Kevex Image Analysis System). The combination of both methods detect changes in focal length and light scattering. On the basis of these results, these techniques can be used in animal studies for grading lenses by functional properties to complement morphologically based grading (slit-lamp) of cataracts provided by a veterinary pathologist.

Animals↗

PubMed1987

Purification and comparative studies of alcohol dehydrogenases.

Alcohol dehydrogenases from various animal and plant sources were purified by a common procedure which employed DEAE, Sephadex-G100 and affinity chromatographies. The procedure achieves an 80-130 fold purification for animal enzymes. However, only a 5-15 fold purification for plant enzymes was attained because of the instability of these enzymes. Purified alcohol dehydrogenases from animal and plant sources differ in coenzyme and substrate specificities. The enzymes from mammalian, avian and fish livers display aldehyde oxidizing and esterolytic activities in addition to alcohol oxidizing activity. However, the enzymes from plants and yeast show only the oxidative activity toward alcohols. Chemical modifications have been performed to identify amino acid residues which are essential to the oxidative and esterolytic activities of alcohol dehydrogenases.

Alcohol Oxidoreductases↗