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Biomedical subjects

T Wood

Publications and source records attributed to T Wood.

At least 109 records · Page 6Linked to original sources
PubMed1975

Formed element deposition onto filtering walls.

Particles are expected to deposit onto filtering surfaces provided the non-dimensional parameter (see article) U (see article) R2S3/2 exceeds a certain value. For erythrocytes this value has a measured value of 0.15, and for platelets the value ranges from 0.01 to 0.15. If deposition is expected, the rate of particle deposition is proportional to the ultrafiltration flow rate. However, the other fluid mechanic mechanisms may transport a greater number of platelets to the surface. We expect these platelets will be fluid mechanically held to the surface even if it is non-sticky for platelets.

Adhesiveness↗
PubMed1974

Catalysis of pentose phosphate pathway reactions by cytoplasmic fractions from muscle, uterus and liver of the rat, and the presence of a reduced nicotinamide-adenine dinucleotide phosphate-triose phosphate oxidoreductase in rat muscle.

1. The enzymes of the pentose phosphate pathway were assayed in supernatant fractions from rat muscle, liver and uterus. 2. On incubation of ribose 5-phosphate with uterus and liver supernatants, triose phosphate, sedoheptulose 7-phosphate and hexose monophosphate accumulated. 3. When a muscle supernatant was used, glycerol 3-phosphate instead of triose phosphate appeared and there was a negligible accumulation of hexose monophosphate. 4. Hexose monophosphate production from ribose 5-phosphate was also followed by measuring NADP(+) reduction in the presence of an excess of phosphoglucose isomerase, glucose 6-phosphate dehydrogenase and 6-phosphogluconate dehydrogenase. 5. With a muscle supernatant, NADPH was reoxidized as rapidly as it was formed owing to the presence of a NADPH-triose phosphate oxidoreductase. 6. A modification of the pentose phosphate pathway in skeletal muscle incorporating this enzyme is proposed.

Animals↗