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Biomedical subjects

D Robinson

Publications and source records attributed to D Robinson.

At least 559 records · Page 31Linked to original sources
PubMed1971

Enzyme purification by electrodecantation.

1. Electrodecantation has been applied to the initial fractionation from crude material of pig kidney beta-d-glucosidase and sheep testicular N-acetylglucosaminidase. 2. The isoelectric points determined by isoelectric focusing were pH4.9 for the beta-d-glucosidase and pH6.3 for the N-acetylglucosaminidase. 3. Electrodecantation of pig kidney extract and sheep testicular extract was carried out at pH4.9 and 6.3 respectively. 4. A six- to ten-fold increase in specific activity could be obtained with good recoveries after a single cycle of electrodecantation. 5. The technique has also been used to purify further an extracellular Bacillus subtilis protease preparation. 6. Attempts to use electrodecantation for the concentration of very dilute enzyme solutions resulted in considerable loss of activity. 7. The limitations and potential use of the technique in laboratory-scale enzyme preparation are discussed.

Acrylates↗
PubMed1971

The distribution of some hydrolases in glomeruli and tubular fragments prepared from rat kidney by zonal centrifugation.

1. A collagenase digest of rat kidney cortex was separated into four bands by zonal centrifugation. 2. Two of these bands were shown by light-microscopy to contain glomeruli and tubular fragments, which were free from each other and well separated from other renal material. 3. Protein, N-acetyl-beta-glucosaminidase, 5'-nucleotidase, l-leucine beta-naphthylamidase, leucine aminopeptidase, acid phosphatase and alkaline phosphatase were assayed across the gradient. 4. The greater proportion of these enzyme activities was recovered in the tubular fragments and acid phosphatase was the only enzyme detected in significant amounts in the glomeruli. 5. Tubular fragments and glomeruli were sedimented and multiple forms of beta-naphthylamidase, N-acetyl-beta-glucosaminidase, acid phosphatase and alkaline phosphatase were investigated by starch-gel electrophoresis.

Acid Phosphatase↗