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Biomedical subjects

G Watson

Publications and source records attributed to G Watson.

At least 109 records · Page 6Linked to original sources
PubMed1977

Binding properties of serum vitamin D transport proteins in vertebrates for 24R, 25-dihydroxycholecalciferol and 24S, 25-dihydroxycholecalciferol in vitro.

1. The affinities of the specific vitamin D plasma transport proteins for 25-hydroxycholecalciferol, 24R, 25-dihydroxycholecalciferol and 24S, 25-dihydroxycholecalciferol were studied in 34 vertebrate species. 2. Fish plasma proteins bound 25-hydroxycholecalciferol, 24R, 25-dihydroxycholecalciferol and 24S, 25-dihydroxycholecalciferol with equal efficiency. 3. Vitamin D transport proteins in birds and a monotreme bound 25-hydroxycholecalciferol more efficiently than 24R, 25-dihydroxycholecalciferol; in one bird the two seco-steroids were bound with equal efficiency. 4. Transport proteins from marsupial and placental mammals bound 24R, 25-dihydroxycholecalciferol more efficiently than 24S, 25-dihydroxycholecalciferol. 5. Twelve mammal transport proteins bound 25-hydroxycholecalciferol and 24R, 25-dihydroxycholecalciferol with equal efficiency, however, in six mammals 25-hydroxycholecalciferol was more efficiently bound.

24,25-Dihydroxyvitamin D 3↗
PubMed1977

Vitamin D2 in vertebrate evolution.

1. The affinities of the specific vitamin D plasma transport proteins for 25-hydroxyergocalciferol and 25-hydroxycholecalciferol were studied in sixty three vertebrate species. 2. Fish, reptile, bird and monotreme plasma proteins bound 25-hydroxyergocalciferol considerably less efficiently than 25-hydroxycholecalciferol. 3. Vitamin D transport proteins from twenty-two placental mammals bound 25-hydroxyergocalciferol and 25-hydroxycholecalciferol with equal efficiency. 4. Proteins from nine mammals bound 25-hydroxycholecalciferol 10-30% more efficiently than 25-hydroxyergocalciferol.

Animals↗
PubMed1976

A training sequence for low vision patients.

A structured training program for teaching low vision patients to efficiently use their optical aids for reading tasks is presented. The arguments for the use of this particular training sequence is supported through the sample patient histories. The training sequences can be developed in any low vision practice and the materials are readily available. The importance of training in a low vision program is emphasized.

Adolescent↗
PubMed1976

Retinal degeneration in cats fed casein. II. Supplementation with methionine, cysteine, or taurine.

All cats fed a taurine-free casein diet for 23 weeks have shown a nondetectable electroretinogram (ERG) in association with a plasma and retinal taurine deficiency. In the present study, the casein diet was supplemented with either taurine or taurine precursors (methionine or cysteine) for 23 weeks to see if retinal function would be preserved. Cats fed the casein diet supplemented with methionine or cysteine showed ERG's reduced in amplitude and delayed in implicit time and had plasma and retinal taurine levels that were well below normal by 23 weeks. Only those cats given taurine in the diet (i.e., those fed chow or casein supplemented with taurine) retained normal ERG function and normal plasma and retinal taurine concentrations. These findings establish a role for taurine in maintaining normal retinal function in the cat.

Animals↗
PubMed1971

Isolation and characterization of an Escherichia coli bacteriophage requiring cell wall galactose.

A new coliphage, designated U3, has been selected for the ability to discriminate the presence of galactose in the cell wall of Escherichia coli. U3 attacks E. coli K-12 cells that are able to incorporate galactose into their cell walls, but mutants blocked in the synthesis of uridine diphosphogalactose, the precursor of cell wall galactose, are completely resistant to the phage. U3 is a small, tail-less, approximately spherical phage resembling phiX174 in its physical properties. Its diameter by electron microscopy is 21 to 22 nm, and its particle weight is approximately 4 x 10(6) daltons. Like phiX174, U3 appears to have a single-stranded deoxyribonucleic acid genome and has at least four cistrons.

Adsorption↗