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.

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

Seasonal changes in the chemical composision of the red alga Hypnea musciformis

1973 ◽  
Vol 24 (3) ◽  
pp. 275
Author(s):  
AF Abdel ◽  
NM Abed ◽  
M Edrees
Keyword(s):  
Amino Acids ◽  
Molecular Weight ◽  
Chemical Composition ◽  
Seasonal Changes ◽  
Free Amino ◽  
Glucuronic Acid ◽  
Red Alga ◽  
Low Molecular Weight ◽  
Hypnea Musciformis ◽  
Algal Material

Seasonal changes were observed in the chemical composition of the marine red alga Hypnea musciformis. Lipids, cholesterol, and lanosterol were found as constituents of the algal material. No low-molecular weight carbohydrates were found except small amounts of mannitol. The algal hydrolysate was shown to contain galactose, glucose, and xylose in all seasons and was characterized by a high content of glucuronic acid and its lactone in February. Definite seasonal variations were found in the patterns of free amino acids and of amino acid compositions of proteins.

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.

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

scholarly journals Antiradical effect of low-molecular peptides in extracts and hydrolyzates from tissues of water organisms

2015 ◽  
Vol 182 (3) ◽  
pp. 269-276
Author(s):  
Ekaterina P. Karaulova ◽  
Anna I. Chepkasova ◽  
Tatiana N. Slutskaya ◽  
Lidia V. Shulgina ◽  
Eugeny V. Yakush
Keyword(s):  
Amino Acids ◽  
Molecular Weight ◽  
Free Amino Acids ◽  
Free Amino ◽  
Chum Salmon ◽  
Soft Tissues ◽  
Antiradical Activity ◽  
Water Extract ◽  
Mercenaria Mercenaria ◽  
Maximum Activity

Molecular-weight composition of peptides in extracts and hydrolyzates from soft tissues of the clams Corbicula japonica and Mercenaria mercenaria and liver of chum salmon is investigated. Antiradical activity is defined for low-molecular peptides, as well as for high-molecular proteins and free amino acids in the extracts. The maximum activity is detected for the extracts of salmon liver; all protein fractions in the water extract of the liver have antiradical activity. Low-molecular peptides and free amino acids have antiradical activity in all samples. The peptides with molecular weight 4.3 kDa have the highest activity in the water extract from C. japonica (43 units) and the peptides with molecular weight 4.7 kDa - in the water extract from M. mercenaria (5.6 units). After hydrolysis, the portion of low-molecular peptides increases for C. japonica , M. mercenaria , and salmon liver in 22.1, 14.5, and 11.1 %, respectively. Hence antiradical activity for hydrolyzates from C. japonica and M. mercen aria is in 1.9 times higher and for hydrolyzates from salmon liver - in 1.3 times higher than for water extracts from their tissues. Only the peptides with molecular weight 2.8-4.7 kDa have antiradical activity in the hydrolyzates; its value is 1-24 activity units for M. mercenaria ; 13-76 units for C. japonica and about 40 units for the chum salmon liver. Correlation is found between the content of peptides with molecular weight 3-4 kDa in hydrolyzates and their antiradical activity.

scholarly journals Soluble nitrogen compounds in tillering nodes and roots of Dactylis glomerata

2015 ◽  
Vol 43 (1) ◽  
pp. 45-57
Author(s):  
T. Dąbrowska
Keyword(s):  
Amino Acids ◽  
Molecular Weight ◽  
Free Amino ◽  
Dactylis Glomerata ◽  
Weight Fraction ◽  
Crystalline Form ◽  
Nitrogen Compounds ◽  
Low Molecular Weight ◽  
Soluble Nitrogen ◽  
Storage Organs

A characteristic is given of the low molecular weight fraction of nitrogen compounds in tillering nodes and roots of the grass <i>Dactylis glomerata</i> in spring and in autumn. It was found that in vegetative storage organs of <i>Dactylis glomerata</i> glutamic acid with glutamine, aspartic acid with asparagine, alanine and arginine play important roles in the storage of nitrogen. From the free amino acids pool of the tillering nodes and roots item amino acids in crystalline form were isolated and identified.

scholarly journals Compartmentation of free amino acids for protein synthesis in rat liver

1974 ◽  
Vol 140 (3) ◽  
pp. 539-545 ◽  
Author(s):  
Judith Airhart ◽  
Alda Vidrich ◽  
Edward A. Khairallah
Keyword(s):  
Amino Acids ◽  
Protein Synthesis ◽  
Rat Liver ◽  
Free Amino Acids ◽  
Free Amino ◽  
Protein Biosynthesis ◽  
Specific Radioactivity ◽  
Intracellular Pool ◽  
Intracellular Compartments ◽  
Intracellular Amino Acids

The concept that a general intracellular pool serves as the sole precursor of amino acids for protein biosynthesis has been vigorously debated in recent years. To help resolve this controversy, we followed the distribution of intraperitoneally administered [3H]valine in the tRNA and the extracellular and intracellular compartments of rat liver. The specific radioactivity of the valine released from isolated tRNA was 2–3 times higher than that of intracellular valine, suggesting that the intracellular pool cannot be the sole precursor of amino acids used for charging tRNA. In addition, the specific radioactivity of the tRNA was only half that of the extracellular valine. Therefore it is unlikely that the valyl-tRNA is charged exclusively with amino acids derived from the extracellular pool. A model is proposed which stipulates that both extracellular and intracellular amino acids contribute to a restricted compartment that funnels amino acids towards protein biosynthesis.

THE TERMINAL AMINO ACIDS OF WHEAT GLIADIN

1955 ◽  
Vol 33 (10) ◽  
pp. 1463-1466 ◽  
Author(s):  
L. K. Ramachandran ◽  
W. B. McConnell
Keyword(s):  
Amino Acids ◽  
Molecular Weight ◽  
Hydrochloric Acid ◽  
Glutamic Acid ◽  
Aspartic Acid ◽  
Free Amino Acids ◽  
Free Amino ◽  
Qualitative Evidence ◽  
Wheat Gliadin ◽  
Terminal Amino

Wheat gliadin has been found by two different methods to contain three N-terminal histidine residues for each molecular weight of 27,000. Trace amounts of N-terminal aspartic acid, glutamic acid, alanine, valine, and serine were also detected in the preparation used. Hydrolysis in boiling hydrochloric acid partially destroyed the di-2,4-dinitrophenyl derivative of histidine. Losses of from 5% to 25% occurred depending upon the time and conditions of hydrolysis. Carboxypeptidase did not release free amino acids from wheat gliadin but qualitative evidence for the occurrence of C-terminal glutamic acid and C-terminal "leucine" was obtained.

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