منابع مشابه
Liver lysosomes in protein-starved rats.
I . The feeding of a protein-free diet to adult rats trained to consume their whole day’s food in z h changed the characteristics of hepatic lysosomes immediately upon the onset of protein deficiency combined with calorie deficiency. 2. The nature of the alterations in the characteristics of liver lysosomes were deduced from the faster release of enzymes, swelling of membranes and a change in t...
متن کاملGlycogen synthesis in the perfused liver of starved rats.
identical with the elongation factors of the supernatant, are present in the ribosomal fraction. These factor(s), presumably, are involved in initiation: however, further investigation is required to elucidate this point. Moreover, preliminary results indicate that a fraction with stimulatory activity similar to that described above can be removed from ribosomes with 0.25Marmmonium chloride. Th...
متن کاملInduction of histidine-degrading enzymes in protein-starved rats.
Inbred weanling rats were maintained on diets containing low (6%), medium (lS%), and high (40%) levels of proteins. After 45 days they were killed and the activities of histidine ammonia lyase, urocanase, and histidine pyruvate aminotransferase in liver were assayed. Histidine ammonia lyase increased with age of the rat, and the increase was proportional to the level of protein in the diet. Ani...
متن کاملAdrenergic Receptor in Heart of Starved Rats
Female Wistar-strain rats were starved for14-19days by feeding approximately1/4of the amount consumed by ad libitum fed controls. The body weight was reduced by41% and the heart weight by38% in these starving periods. The 125 I-iodocyanopindrol (ICYP) binding capacity of heart preparations from the starved rats was35.3•}11.1 (mean•}SD) fmol/mg protein in comparison with 69.3•}14.9for the contro...
متن کاملIncreased protein kinase C activity is linked to reduced insulin receptor autophosphorylation in liver of starved rats.
Phosphorylation of the insulin receptor beta-subunit on serine/threonine residues by protein kinase C reduces both receptor kinase activity and insulin action in cultured cells. Whether this mechanism regulates insulin action in intact animals was investigated in rats rendered insulin-resistant by 3 days of starvation. Insulin-stimulated autophosphorylation of the partially purified hepatic ins...
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ژورنال
عنوان ژورنال: British Journal of Nutrition
سال: 1969
ISSN: 0007-1145,1475-2662
DOI: 10.1079/bjn19690087