scholarly journals Metabolism of Sulphur Amino Acids I. the Uptake of Cysteine by Rat Liver

1957 ◽  
Vol 10 (2) ◽  
pp. 217 ◽  
Author(s):  
Eva Eden ◽  
Helen B Granowski ◽  
WG Jones ◽  
Judith A Linnane
Keyword(s):  
Amino Acids ◽  
Rat Liver ◽  
Normal Level ◽  
Intraperitoneal Injection ◽  
Stomach Tube ◽  
Sulphur Amino Acids

Cysteine was administered to rats by stomach tube. or by intraperitoneal injection. In some animals the concentration of glutathione in the liver was first lowered to 10 per cent. of the normal level by injecting the animals with bromobenzene. When 30mg of cysteine were given by stomach tube, 75 per cent. of the cysteine taken up by the liver in normal rats was oxidized in 1 hr to products other than cystine. In animals treated with bromo benzene all the cysteine was converted to glutathione and no increase could be found in the oxidized sulphur fraction. In both groups of animals only traces of cysteine were present.

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.

scholarly journals Ontogenic changes in hepatic glutathione and metallothionein in rats and the effect of a low-sulphur-containing diet

1990 ◽  
Vol 63 (1) ◽  
pp. 97-103 ◽  
Author(s):  
Misako Taniguchi ◽  
M. George Cherian
Keyword(s):  
Amino Acids ◽  
Rat Liver ◽  
Soya Bean ◽  
Protein Diet ◽  
Major Protein ◽  
Newborn Rat ◽  
Pregnant Rats ◽  
Hepatic Glutathione ◽  
Sulphur Amino Acids ◽  
Bean Protein

Metallothionein contains about 30% cysteine and is a major protein in newborn rat liver. This protein and glutathione constitute two major intracellular cysteine pools in newborn rat liver. When pregnant rats were fed on a soya-bean-protein diet, low in sulphur amino acids, the hepatic glutathione levels of the dams were decreased. However, this did not affect the levels of glutathione or metallothionein in the pups. The activity of the glutathione-degrading enzyme γ-glutamyltransferase (EC2.3.2.2) in the livers of pups was maximum at birth and gradually decreased with age when the hepatic glutathione was transported to the kidney. In the pups born from dams fed on soya-bean-protein diet the decline in the hepatic enzyme activity was delayed, suggesting a continued degradation of glutathione in the liver. These results suggest that even with a maternal nutritional deficiency of sulphur amino acids, the transfer of cysteine to the fetus is not impaired. However, the hepatic intra-organ degradation of glutathione is continued in these pups for a prolonged period after birth compared with pups born from control mothers. The increased degradation of glutathione in the liver may be essential to meet the requirement of cysteine in pups born from dams fed on the soya-bean-protein diet.

scholarly journals Cell swelling inhibits proteolysis in perfused rat liver

1990 ◽  
Vol 272 (1) ◽  
pp. 239-242 ◽  
Author(s):  
D Häussinger ◽  
C Hallbrucker ◽  
S vom Dahl ◽  
F Lang ◽  
W Gerok
Keyword(s):  
Amino Acids ◽  
Rat Liver ◽  
Liver Cell ◽  
Intraperitoneal Injection ◽  
Branched Chain Amino Acids ◽  
Cell Swelling ◽  
Perfused Rat Liver ◽  
Close Relationship ◽  
Branched Chain

Exposure of isolated single-pass-perfused rat liver to hypo-osmotic media resulted in liver cell swelling and an inhibition of release of branched-chain amino acids. Similarly, cell swelling inhibited [3H]leucine release from perfused livers from rats in which liver proteins were prelabelled in vivo by intraperitoneal injection of L-[4,5-3H]leucine 16-20 h before the experiment. The effects of cell swelling on [3H]leucine release were fully reversible. [3H]Leucine release was also inhibited when cell swelling was induced by addition of glutamine (0.5-2 mM). There was a close relationship between the inhibition of [3H]leucine release and the degree of liver cell swelling, regardless of whether cell swelling was induced by hypo-osmotic perfusion or addition of glutamine. The data suggest that the known anti-proteolytic effect of glutamine is in large part due to glutamine-induced hepatocyte swelling.

scholarly journals Alterations of lysosomal size and density during rat liver perfusion. Suppression by insulin and amino acids.

1977 ◽  
Vol 252 (19) ◽  
pp. 6948-6954 ◽  
Author(s):  
A N Neely ◽  
J R Cox ◽  
J A Fortney ◽  
C M Schworer ◽  
G E Mortimore
Keyword(s):  
Amino Acids ◽  
Rat Liver ◽  
Liver Perfusion ◽  
Rat Liver Perfusion

EFFECTS OF HYPOGLYCIN A ON THE METABOLISM OF AMINO ACIDS BY LIVER SLICES

1964 ◽  
Vol 42 (1) ◽  
pp. 139-142 ◽  
Author(s):  
S. J. Patrick ◽  
L. C. Stewart
Keyword(s):  
Amino Acids ◽  
Fatty Acids ◽  
Fatty Acid ◽  
Glutamic Acid ◽  
Rat Liver ◽  
Inhibitory Effects ◽  
Liver Slices

The effects of hypoglycin A on the metabolism of L-leucine-C14, L-alanine-C14, and L-glutamic-acid-C14 by rat liver slices have been investigated. Hypoglycin exerted markedly inhibitory effects on the conversion of leucine-C14 to fatty acid, cholesterol, and CO2. Conversion of alanine-C14 and glutamic acid-C14 to fatty acids was also inhibited by hypoglycin. No effects of hypoglycin on the conversion of C14-amino acids into protein or glycogen were demonstrated.

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