Academic
Publications
Rat Liver Histidase: Glucose Repression and Half-life after Casein Hydrolysate Feeding

Rat Liver Histidase: Glucose Repression and Half-life after Casein Hydrolysate Feeding,SHIH CHING LEE,JEAN K. TEWS,MARGOT L. MORRIS,E. HARPER

Rat Liver Histidase: Glucose Repression and Half-life after Casein Hydrolysate Feeding   (Citations: 1)
BibTex | RIS | RefWorks Download
Histidase, the first enzyme in the major catabolic pathway of histidine, increases in animals fed a large quantity of amino acids but the induc tion is suppressed if glucose is fed with the amino acids. This investigation was undertaken to determine whether glucose suppression would be influenced by glucagon or cyclic adenosinemonophosphate (c-AMP). Hepatic histidase activity of protein-depleted rats increased twofold within 16 hours after they were force- fed casein hydrolysate, but the increase was prevented if they were force-fed glucose at the same time. Administration of glucagon or dibutyryl cyclic AMP to protein-depleted rats also increased histidase activity, and administration of either of these substances counteracted the glucose repression. The hepatic histi dase activity was elevated in alloxan-diabetic rats but decreased significantly when the diabetic animals were treated with insulin. The concentration of liver cyclic AMP increased in rats force-fed casein hydrolysate but not when glucose and casein hydrolysate were fed together. These results suggest that cyclic AMP is involved in the induction of histidase by casein hydrolysate and suppression of this response by force-feeding glucose. The apparent half-life of hepatic histi dase in protein-depleted rats force-fed casein hydrolysate was 2.1 days, com parable to the value obtained from measurements on rats fed ad libitum an 80% casein diet for 14 days. Total liver histidase activity was maintained in rats starved for 5 days although total liver protein decreased. J. Nutr. 102: 319-330, 1972.
Published in 2010.
Cumulative Annual
View Publication
The following links allow you to view full publications. These links are maintained by other sources not affiliated with Microsoft Academic Search.
Sort by: