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R Hoffenberg

Publications and source records attributed to R Hoffenberg.

At least 91 records · Page 5Linked to original sources
PubMed1974

The identification of 3,3', 5,5',-tetraiodothyroformic acid within the rat liver.

Homogenized rat livers were extracted with organic solvents and the extracts converted into more readily volatile derivatives (trimethylsilylmethyl esters and permethyl esters). Combined g.l.c.-mass-spectrometric analysis identified the presence of tetraiodothyroformate. It is postulated that mitochondrial beta-oxidation of tetraiodothyropyruvate results in the formation of this apparently undescribed metabolite.

Animals↗
PubMed1973

Triiodothyronine.

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Biological Transport↗
PubMed1971

Albumin synthesis by the perfused rat liver. A comparison of methods with special reference to the effect of dietary protein deprivation.

1. Isolated perfused rat livers were used to study synthesis of albumin after donors had been fed on normal or protein-free diets. 2. Methods of determining the liver's ability to produce albumin included incorporation of [(14)C]carbonate, [(3)H]lysine and [(14)C]arginine, as well as a direct method based on a heterologous perfusing system of rat erythrocytes and rabbit plasma. 3. Livers from protein-deprived rats were found to form extremely little urea and not to incorporate (14)CO(2) into [(14)C]urea, but they were capable of producing [(14)C]urea from [(14)C]arginine and of incorporating the latter and [(3)H]lysine into albumin. 4. By immunological means these lives were found to synthesize less albumin than normal, but their ability was only slightly impaired when related to body weight or liver weight. 5. These findings are consistent with a block in urea-cycle enzymes with relative integrity of arginase activity and of amino acid activation.

Animals↗
PubMed1970

Plasma protein catabolism by the perfused rat liver. The effect of alteration of albumin concentration and dietary protein depletion.

1. The isolated perfused rat liver was used to study degradation rates of plasma albumin, transferrin and fibrinogen. 2. Constant fractional rates were observed for all three proteins even when the albumin concentration was drastically increased by the addition of large amounts to the perfusate pool. 3. Livers taken from rats deprived of dietary protein for 14-18 days showed greatly diminished fractional catabolic rates for albumin when perfused with blood from similarly deprived animals. 4. These rates could be restored to near-normal values by adding albumin or by perfusing with blood from normally fed rats. 5. These findings are consistent with the theory of pinocytosis as a step in the degradation of plasma proteins by hepatic parenchymal cells.

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