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Biomedical subjects

A Grossman

Publications and source records attributed to A Grossman.

At least 307 records · Page 17Linked to original sources

Tyrosine aminotransferase converting factor: kinetic properties, cellular localization, and tissue distribution.

Utilizing a more rapid procedure for determining tyrosine aminotransferase-converting factor activity, the kinetic properties of this factor were characterized further. Tyrosine aminotransferase-converting factor is a heat-labile substance present in the particulate fraction of rat liver that converts tyrosine aminotransferase form III to I at 4 degrees C. Analysis of the distribution of marker enzymes for mitochondria and lysosomes, and of converting factor, following differential and discontinuous sucrose gradient centrifugation indicated that this factor was associated with light lysosomes. The activity of converting factor was not altered following administration of cortisol. Converting factor activity, equivalent to that in liver, was also observed in particulate fractions from kidney and spleen, and to a lesser extent, in pancreas and salivary gland. No detectable activity was observed in brain, heart, small intestine, skeletal muscle, red blood cells, serum, or plasma. The presence of converting factor activity in kidney and spleen suggests that other proteins are substrates for this factor since tyrosine aminotransferase is virtually absent from these tissues. Alternatively, the absence of converting factor from other tissues need not indicate they are devoid of converting factor-like activity merely, that such activity in these tissues has different specificities and does not utilize tyrosine aminotransferase as a substrate.

Animals↗

A new technique for the treatment of guilt.

A behavioural technique is described suitable for the treatment of patients with high levels of guilt who attempt to relieve their depression by risk-taking activities which reflect their individual wishes and fears, or who suffer anxiety due to unacceptable past behaviour. It is recommended as an alternative brief method of treatment to psychoanalysis and is based on the application of behaviour therapy to a patient's psychopathology. Three case histories are described to illustrate the principles of the technique.

Adult↗

Regulation of glucose 6-phosphate dehydrogenase in blue-green algae.

Glucose 6-phosphate dehydrogenase (EC 1.1.1.49) has been partially purified from Anacystis nidulans and Anabaena flos-aquae by means of ammonium sulfate fractionation and exclusion gel chromatography and the kinetic properties determined.Glucose 6-phosphate dehydrogenase from these blue-green algae exhibits Michaelis-Menten kinetics at pH 6.7. At this pH, Km values of 0.37 mm for glucose 6-phosphate and 10 mum for NADP were determined. At a pH above 7.4, the enzyme exhibits sigmoidal kinetics with respect to glucose 6-phosphate saturation but the saturation curve for NADP remains hyperbolic.ATP is an inhibitor of the enzyme competitively with NADP with a Ki of 2 to 5 mm. NADPH inhibits the enzyme competitively with glucose 6-phosphate. The inhibition curves for NADPH are hyperbolic at pH 6.7 and sigmoidal at pH 8.6.The significance of these in vitro kinetics are discussed relative to in vivo data on the control of glucose 6-phosphate turnover in blue-green algae.

Journal Article↗

Biochemical confirmation of an experimental osteoarthritis model.

Section of the medial collateral and both cruciate ligaments combined with resection of the medial meniscus in rabbit knees caused instability and during the ensuing six months these knees showed progressive histological changes similar to those of human osteoarthritis. Biochemical analysis of the cartilage from such knee joints demonstrated a decrease in proteoglycan, an increase in acid phosphatase, and increases in the rates of synthesis of protein and glycosaminoglycan. These findings, which are quite consistent with those in human osteoarthritis, suggest that this animal model may be of value in the study of the pathogenesis and treatment of human disease.

Acid Phosphatase↗