scholarly journals Compartmentation of albumin and ferritin synthesis in rat liver in vivo

1976 ◽  
Vol 156 (1) ◽  
pp. 189-192 ◽  
Author(s):  
E B Fern ◽  
P J Garlick
Keyword(s):  
Amino Acids ◽  
Rat Liver ◽  
Free Amino Acids ◽  
Free Amino ◽  
Plasma Albumin ◽  
Ferritin Synthesis ◽  
Liver Ferritin ◽  
Ferritin Synthesis In

Infusion of rats with [U-14C]glycine resulted in labelling of glycine and serine in plasma albumin and liver ferritin. The patterms of labelling in these two proteins were not similar, suggesting that each is synthesized from a different pool of free amino acids.

scholarly journals Amino acid regulation of synthesis of ribonucleic acid and protein in the liver of rats

1971 ◽  
Vol 124 (2) ◽  
pp. 385-392 ◽  
Author(s):  
R. W. Wannemacher ◽  
C. F. Wannemacher ◽  
M. B. Yatvin
Keyword(s):  
Amino Acids ◽  
Protein Synthesis ◽  
Free Amino Acids ◽  
Free Amino ◽  
Cellular Protein ◽  
Deficient Diet ◽  
Cellular Protein Content ◽  
Regulate Protein

Weanling (23-day-old) rats were fed on either a low-protein diet (6% casein) or a diet containing an adequate amount of protein (18% casein) for 28 days. Hepatic cells from animals fed on the deficient diet were characterized by markedly lower concentrations of protein and RNA in all cellular fractions as compared with cells from control rats. The bound rRNA fraction was decreased to the greatest degree, whereas the free ribosomal concentrations were only slightly less than in control animals. A good correlation was observed between the rate of hepatic protein synthesis in vivo and the cellular protein content of the liver. Rates of protein synthesis both in vivo and in vitro were directly correlated with the hepatic concentration of individual free amino acids that are essential for protein synthesis. The decreased protein-synthetic ability of the ribosomes from the liver of protein-deprived rats was related to a decrease in the number of active ribosomes and heavy polyribosomes. The lower ribosomal content of the hepatocytes was correlated with the decreased concentration of essential free amino acids. In the protein-deprived rats, the rate of accumulation of newly synthesized cytoplasmic rRNA was markedly decreased compared with control animals. From these results it was concluded that amino acids regulate protein synthesis (1) by affecting the number of ribosomes that actively synthesize protein and (2) by inhibiting the rate of synthesis of new ribosomes. Both of these processes may involve the synthesis of proteins with a rapid rate of turnover.

Studies on pathogenesis of experimental fatty liver (I) variation in the pattern of free amino acids of albino rat liver

1966 ◽  
Vol 1 (1) ◽  
pp. 38-39
Author(s):  
Y. Takaoka ◽  
K. Yokouchi ◽  
G. Mitsuoka ◽  
H. Tajima ◽  
E. Uchiyama ◽  
...  
Keyword(s):  
Amino Acids ◽  
Fatty Liver ◽  
Rat Liver ◽  
Free Amino Acids ◽  
Free Amino ◽  
Albino Rat

Correlation between osmoregulation and cell volume regulation

1987 ◽  
Vol 252 (4) ◽  
pp. R768-R773
Author(s):  
M. A. Lang
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Osmotic Pressure ◽  
Cell Volume ◽  
Free Amino Acids ◽  
Volume Regulation ◽  
Free Amino ◽  
Cell Volume Regulation

The euryhaline crab, Callinectes sapidus, behaves both as an osmoregulator when equilibrated in salines in the range of 800 mosM and below and an osmoconformer when equilibrated in salines above 800 mosM. There exists a close correlation between osmoregulation seen in the whole animal in vivo and cell volume regulation studied in vitro. Hyperregulation of the hemolymph osmotic pressure and cell volume regulation both occurred in salines at approximately 800 mosM and below. During long-term equilibration of the crabs to a wide range of saline environments, the total concentration of hemolymph amino acids plus taurine remained below 3 mM. During the first 6 h after an acute osmotic stress to the whole animal, the hemolymph osmotic pressure and Na activity gradually decreased, whereas the free amino acids remained below 3 mM. As the hemolymph osmotic pressure decreased below approximately 850 mosM, the amino acid level began to increase to 17-25 mM. This change was primarily due to increases in glycine, proline, taurine, and alanine. The likely source of the increase in hemolymph free amino acids in vivo is the free amino acid loss from muscle cells observed during cell volume regulation in vitro.

scholarly journals THE CHEMISTRY OF INSECT HEMOLYMPH

1956 ◽  
Vol 39 (6) ◽  
pp. 853-868 ◽  
Author(s):  
G. R. Wyatt ◽  
T. C. Loughheed ◽  
S. S. Wyatt
Keyword(s):  
Amino Acids ◽  
Free Amino Acids ◽  
Free Amino ◽  
Developmental Stages ◽  
Galleria Mellonella ◽  
Similar Distribution ◽  
Total Acid ◽  
Protein Nitrogen ◽  
Larval Hemolymph

1. Hemolymph was collected for analysis from the silkworm, Bombyx mori, in a series of developmental stages ranging from the second molt to the late pupa. The mean pH of larval hemolymph after collection was found to be 6.45, that of pupal hemolymph, 6.57; in vivo values may be slightly lower. Total dry solids ranged from 5.4 to 10.6 per cent. Total protein ranged from 1.2 to 5.3 per cent, increasing rapidly during the fifth instar. 2. Free amino acids were separated chromatographically and estimated. Of 19 amino acids identified, amounting collectively to 823 to 1497 mg. per 100 ml., glutamine, histidine, and lysine generally occurred in greatest amount. Tryptophan was not detected, and cystine (or cysteine) was found in only one sample. The total free amino acids account for 35 to 55 per cent of the non-protein nitrogen of the plasma. 3. Free sugars, estimated semiquantitatively on chromatograms, comprise glucose, fructose, and sucrose in total amount ranging from about 5 to 40 mg. per 100 ml. Total acid-soluble, ultrafiltrable carbohydrate, estimated as glucose by the anthrone reaction, ranged from 166 to 635 mg. per 100 ml., indicating the presence of low molecular weight sugar derivatives. 4. Inorganic phosphate amounted to 5 to 15 mg. per 100 ml., and acid-soluble organic phosphate to 100 to 200 mg. per 100 ml. The latter fraction includes several substances, of which one was tentatively identified as glucose-6-phosphate and the remainder are as yet unidentified. 5. Single samples of hemolymph were also taken from larvae of the wax moth, Galleria mellonella, and the spruce sawfly, Diprion hercyniae. These contained even higher concentrations of solutes than the silkworm samples, but with a generally similar distribution. The proportions of the free amino acids were different in each species.

Free amino acids of Nicotiana alata anthers during development in vivo

1983 ◽  
Vol 57 (4) ◽  
pp. 527-531 ◽  
Author(s):  
Helle Krogaard ◽  
A. Skytt Andersen
Keyword(s):  
Amino Acids ◽  
Free Amino Acids ◽  
Free Amino ◽  
Nicotiana Alata

scholarly journals Free amino acids of testes. Concentrations of free amino acids in the testes of several species and the precursors of glutamate and glutamine in rat testes in vivo

1973 ◽  
Vol 132 (3) ◽  
pp. 353-359 ◽  
Author(s):  
Isa K. Mushahwar ◽  
Roger E. Koeppe
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Guinea Pig ◽  
Free Amino Acids ◽  
Free Amino ◽  
Ammonium Acetate ◽  
Testicular Tissue ◽  
Species Variation

Determination of the free amino acid and lactate content of testicular tissue in rat, guinea pig, rabbit, cat, gerbil, hamster, chicken and bullfrog indicates a substantial species variation. Insulin hypoglycaemia and ammonium acetate toxicity changes the concentration of several free amino acids of rat testes. 14C radioactivity from labelled acetate and ethanol is rapidly incorporated into some of the free amino acids of rat testes in vivo, whereas incorporation from [14C]glucose is relatively slow. These results have been compared with those obtained from similar studies with rat brain. In contrast to brain, there is no evidence for glutamate compartmentation in testes.

In vivo oocyte hydration in Atlantic halibut (Hippoglossus hippoglossus); proteolytic liberation of free amino acids, and ion transport, are driving forces for osmotic water influx

2002 ◽  
Vol 205 (2) ◽  
pp. 211-224
Author(s):  
Roderick Nigel Finn ◽  
Gunn C. Østby ◽  
Birgitta Norberg ◽  
Hans Jørgen Fyhn
Keyword(s):  
Amino Acids ◽  
Free Amino Acids ◽  
Free Amino ◽  
Driving Forces ◽  
Atlantic Halibut ◽  
Hippoglossus Hippoglossus ◽  
Oocyte Hydration ◽  
Osmotic Water ◽  
Cellular Water

SUMMARY The in vivo swelling and hydration of maturing oocytes of Atlantic halibut Hippoglossus hippoglossus were studied in order to characterise the osmotic mechanism underlying oocyte hydration in oviparous marine teleosts that spawn pelagic eggs. Sequential biopsies from two females, spanning four hydration cycles, were examined by osmometry, solute analysis and electrophoresis of dissected hydrating oocytes and ovulated eggs. The hydration cycle of the biopsied halibuts lasted 33–54 h. The majority of ovarian oocytes existed in a pre-hydrated condition (individual wet mass approx. 3.7 mg, diameter approx. 1.87 mm, 63 % H2O) with easily visible, non-coalesced, yolk platelets. Group-synchronous batches of the pre-hydrated oocytes increased in individual wet mass, diameter and water content to reach the ovulated egg stage of approximately 15 mg, 3.0 mm and 90 % H2O, respectively. The yolk osmolality of the hydrating oocytes was transiently hyperosmotic to the ovarian fluid (range 305–350 mOsmol l–1) with a peak osmolality of about 450 mOsmol l–1 in oocytes of 6–8 mg individual wet mass. The transient hyperosmolality was well accounted for by the increase in oocyte content of free amino acids (FAAs; approx. 2300 nmol oocyte–1), K+ (approx. 750 nmol oocyte–1), Cl– (approx. 900 nmol oocyte–1), total ammonium (approx. 300 nmol oocyte–1) and inorganic phosphate (Pi; approx. 200 nmol oocyte–1) when relating to the increase in cellular water. The oocyte content of Na+ did not increase during the hydration phase. Extensive proteolysis of yolk proteins, in particular a 110 kDa protein, correlated with the increase in the FAA pool, although the latter increased by approx. 20 % more than could be accounted for by the decrease in the oocyte protein content. Both indispensable and dispensable amino acids increased in the FAA pool, and particularly serine, alanine, leucine, lysine, glutamine and glutamate. Taurine content remained stable at approx. 70 nmol oocyte–1 during oocyte hydration. The results show that final hydration of Atlantic halibut oocytes is caused by an osmotic water uptake in which FAAs, derived mainly from the hydrolysis of a 110 kDa yolk protein, contribute approximately 50 % of the yolk osmolality and ions (Cl–, K+, Pi, NH4+) make up the balance.

Rat liver and kidney pools of free amino acids in norm and with different doses of pyrazinamide

2006 ◽  
Vol 164 ◽  
pp. S95
Author(s):  
Larysa B. Bondarenko ◽  
Natalia A. Saprykina ◽  
Valentina M. Kovalenko
Keyword(s):  
Amino Acids ◽  
Rat Liver ◽  
Free Amino Acids ◽  
Free Amino ◽  
Liver And Kidney ◽  
Different Doses

Intracellular low molecular weight iron

1989 ◽  
Vol 17 (3) ◽  
pp. 490-490 ◽  
Author(s):  
N. DEIGHTON ◽  
R. C. HIDER
Keyword(s):  
Amino Acids ◽  
Molecular Weight ◽  
Rat Liver ◽  
Free Amino Acids ◽  
Free Amino ◽  
Low Molecular Weight ◽  
High Affinity ◽  
Chemical Techniques ◽  
Low Molecular Weight Iron

Summary A low molecular weight complex of an iron oligomer (Mr ~ 1000) has been isolated from rat liver and characterized physically and chemically. The h.p.l.c.-purified material contains the free amino acids glutamate and aspartate. Chemical techniques suggest the iron present in the factor is as iron(III) and is readily donated to high-affinity chelators such as the hydroxypyridinones and desferoxamine.

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