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D N Baron

Publications and source records attributed to D N Baron.

At least 73 records · Page 4Linked to original sources
PubMed1974

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Laboratories↗
PubMed1974

Plasma alkaline phosphatase isoenzymes in hepatobiliary disease.

BY CELLULOSE ACETATE OR ACRYLAMIDE GEL ELECTROPHORESIS IT IS POSSIBLE TO SEPARATE THESE ALKALINE PHOSPHATASE ISOENZYMES FROM SERUM: [anode] fast liver, slow liver, placenta/Regan, bone, intestine, bile [cathode]. Heat or chemical inhibition can confirm the differentiation. Normal adult serum always contains slow-liver isoenzyme, and sometimes bone isoenzyme: the latter is always present in serum of children. In hepatobiliary disease slow-liver isoenzyme was always increased: intestinal isoenzyme appeared in many cases of cirrhosis (of blood groups B and 0) but fast-liver and bile isoenzymes were occasionally seen in miscellaneous cases. The findings in other diseases included Regan isoenzyme in six out of 45 cases of malignant disease.

Alkaline Phosphatase↗
PubMed1974

Training and career appointments in the pathological sciences in the United Kingdom.

Pathologists usually receive initial training in clinical work, or in general pathology, or in academic work, followed by speciality training as a senior registrar or lecturer. Consultant status is generally achieved by the age of 34, now almost always in a single discipline. The distribution of pathologists between disciplines, in National Health Service and university posts, is tabulated: there are many unfilled appointments.

Allergy and Immunology↗
PubMed1972

Purification and comparative properties of isoenzymes of nicotinamide-adenine dinucleotide phosphate-isocitrate dehydrogenase from rat heart and liver.

1. Rat liver and heart major isoenzymes of NADP-isocitrate dehydrogenase have each been purified about 100-fold by a combination of ammonium sulphate fractionation and chromatography on ion-exchange cellulose and their properties compared. 2. The properties were similar in respect of pH, inhibition by Hg(2+) and Michaelis constants for isocitrate and NADP. 3. Some of the properties of the isoenzymes were different. 4. The heart isoenzyme was activated about 210% by 0.8m-ammonium sulphate whereas the liver isoenzyme was unaffected. The heart isoenzyme showed greater sensitivity to inactivation by heat (30 degrees C for 30min), whereas the liver isoenzyme was more sensitive to inactivation by p-chloromercuribenzoate and by Cu(2+). 5. The Michaelis constants with 3-acetylpyridine-adenine dinucleotide phosphate showed a twofold difference between liver and heart isoenzyme. 6. The differential sensitivity to heat and its mainly non-cytoplasmic location may be an explanation of the failure of plasma isocitrate dehydrogenase activity to increase after a myocardial infarction.

Animals↗