scholarly journals The effect of hypophysectomy of the rat and of treatment with growth hormone on the incorporation in vivo of radioactive amino acids into the proteins of subcellular fractions of rat liver

1960 ◽  
Vol 74 (3) ◽  
pp. 462-471 ◽  
Author(s):  
A Korner
Keyword(s):  
Amino Acids ◽  
Growth Hormone ◽  
Rat Liver ◽  
Subcellular Fractions

scholarly journals Effects of the hepatotoxic agents retrorsine and aflatoxin B1 on hepatic protein synthesis in the rat

1968 ◽  
Vol 109 (1) ◽  
pp. 87-91 ◽  
Author(s):  
S. Villa-Treviño ◽  
D. D. Leaver
Keyword(s):  
Amino Acids ◽  
Protein Synthesis ◽  
Rat Liver ◽  
Aflatoxin B1 ◽  
Plasma Proteins ◽  
Pyrrolizidine Alkaloid ◽  
Main Site ◽  
Nuclear Rna ◽  
Hepatic Protein Synthesis

1. Aflatoxin and the pyrrolizidine alkaloid retrorsine inhibited the incorporation of labelled amino acids into rat liver and plasma proteins in vivo. Inhibition was greater and detected earlier with retrorsine (1hr.) than with aflatoxin (3hr.). 2. Both toxins affected the liver ribosomal aggregates, causing increases in the proportion of monomers plus dimers. The effect of retrorsine was greater than that of aflatoxin. 3. Incorporation of labelled amino acids into proteins of cell-free preparations of liver from rats treated with aflatoxin was lower than in control preparations. The main site of inhibition appeared to be the ribosomes. 4. Both toxins inhibited the incorporation of orotate into liver nuclear RNA 1hr. after administration.

Proteinsynthese in grünen Blättern

1964 ◽  
Vol 19 (3) ◽  
pp. 235-248 ◽  
Author(s):  
Benno Parthier
Keyword(s):  
Amino Acids ◽  
Specific Activity ◽  
Subcellular Fractions ◽  
Mechanical Destruction ◽  
Cell Organization ◽  
Specific Activities ◽  
Short Time ◽  
Natural Cell

In the green leaves of Nicotiana rustica, protein synthesis of various subcellular fractions has been investigated in vivo after 14CO2-photosynthesis and also in vitro by incorporation of radioactive amino acids. Following photosynthesis, homogenization of the tissues, and differential centrifugation of the homogenates, the results show that all structural particles of the cell are able to use photosynthetically formed amino acids for the incorporation into their proteins. The proteins with the highest specific activities are found in the mitochondria-rich fractions, and with the lowest in the soluble cytoplasma supernatant. High specific activities are also observed in the ribosomal-rich fraction in short-time experiments, and also in the chloroplasts after exposure of the leaves to light. After an osmotic-mechanical destruction of the isolated 14C-labelled chloroplasts, the specific activities of lamellar proteins exceed the colourless soluble proteins of the chloroplasts. A green fraction, sedimented at 1,000 g, and perhaps mainly consisting of broken and leached chloroplasts, shows the highest specific activity of all chloroplast fractions. Obviously, due to the destruction of the natural cell organization, in vitro experiments give not only drastically decreased specific activities but also another distribution of the incorporated amino acids between the subcellular fractions, compared with experiments in vivo.

scholarly journals A procedure for the quantitative analysis of the sulphur amino acids of rat tissues

1967 ◽  
Vol 102 (3) ◽  
pp. 959-975 ◽  
Author(s):  
M. K. Gaitonde ◽  
G. E. Gaull
Keyword(s):  
Amino Acids ◽  
Rat Liver ◽  
Rat Tissues ◽  
Sulphur Compounds ◽  
One Dimensional ◽  
Quantitative Separation ◽  
Exchange Resins ◽  
Sulphur Amino Acids ◽  
Dowex 1

1. A method is described for the quantitative separation of the sulphur compounds in a single sample of tissue by passing an extract through a serial assembly of ion-exchange resins in the order: Dowex 2 (Cl(-) form), Dowex 1 (CO(3) (2-) form), Amberlite CG-50 (H(+) form) and Zeo-Karb 225 (H(+) form). 2. Groups of sulphur amino acids were eluted separately from each column; the recovery of sulphur compounds after their labelling with (35)S in vivo by injection of l-[(35)S]-methionine was 91-106%. Individual sulphur compounds were further resolved by one-dimensional or two-dimensional paper chromatography. 3. Evidence is presented on the occurrence of S-adenosylmethionine and S-adenosylhomocysteine in rat liver and brain. Rat liver and brain contained 83.6 and 31.4mmu-moles/g. respectively of S-adenosylmethionine.

In vivo interaction of human growth hormone (HGH) with subcellular structures of rat liver

1978 ◽  
Vol 12 (11) ◽  
pp. 1087
Author(s):  
M C POSTEL-VINAY ◽  
C KAYSER ◽  
B DESBUQUOIS
Keyword(s):  
Growth Hormone ◽  
Rat Liver ◽  
Human Growth Hormone ◽  
Human Growth

scholarly journals Albumin, fibrinogen and transferrin synthesis in isolated rat hepatocyte suspensions. A model for the study of plasma protein synthesis

1975 ◽  
Vol 146 (1) ◽  
pp. 141-155 ◽  
Author(s):  
K N Jeejeebhoy ◽  
J Ho ◽  
G R Greenberg ◽  
M J Phillips ◽  
A Bruce-Robertson ◽  
...  
Keyword(s):  
Amino Acids ◽  
Growth Hormone ◽  
Protein Synthesis ◽  
Plasma Protein ◽  
Plasma Proteins ◽  
Horse Serum ◽  
Rat Hepatocyte ◽  
Isolated Rat

A system using hepatocyte suspensions in vitro was developed for studying the synthesis of albumin, fibrinogen and transferrin. Conditions for optimum survival of the hepatocyte and for synthesis of these plasma proteins were defined for this system. These conditions included the use of horse serum (17.5 percent, v/v, heat-inactivated), an enriched medium (Waymouth's MB 752/1), an O2 tension of between 18.7 times 10(3) and 26.7 times 10(3) Pa and constant stirring. Albumin, fibrinogen and transferrin synthesis rates were obtained of 0.32 p 0.094(10), 0.12 p 0.030(11) and 0.097 p 0.017(10) [mean p S.D. (n)]mg/h per g of hepatocytes respectively. These rates were maintained for the first 12h of study and synthesis continued at a diminished rate up to 48h. The synthesis of albumin was decreased in a medium containing less amino acids and glucose, but that of fibrinogen was substantially unaffected. ATP concentrations up to 12h and RNA/DNA ratios up to 24h were comparable with values in vivo. The ability to study cells up to 48h permitted us to find that the addition of a mixture of hormones consisting of glucagon, cortisol, tri-iodothyronine and growth hormone enhanced fibrinogen synthesis. Addition of insulin to the above mixture resulted in increased synthesis for albumin and transferrin but not for fibrinogen.

scholarly journals Distribution of 3H-acetyl Growth Hormone (3H-HGH) in the Subcellular Fractions of Rat Liver

1970 ◽  
Vol 4 (5) ◽  
pp. 457-458
Author(s):  
Vaddanahally T Maddaiah ◽  
Iraj Rezvani ◽  
Shang Y Chen ◽  
Platon J Collipp
Keyword(s):  
Growth Hormone ◽  
Rat Liver ◽  
Subcellular Fractions

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.

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