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.

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.

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.

Difunctional enols of N-protected amino acids as low molecular weight and novel inhibitors of HIV-1 protease.

1993 ◽  
Vol 3 (6) ◽  
pp. 1169-1174 ◽  
Author(s):  
Marc Vaillancourt ◽  
Benoit Vanasse ◽  
Eric Cohen ◽  
Gilles Sauv
Keyword(s):  
Amino Acids ◽  
Molecular Weight ◽  
Low Molecular Weight ◽  
Hiv 1

STUDIES ON THE ISOLATION AND NATURE OF THE 'TERREGENS FACTOR'

1954 ◽  
Vol 32 (1) ◽  
pp. 400-406 ◽  
Author(s):  
M. O. Burton ◽  
F. J. Sowden ◽  
A. G. Lochhead
Keyword(s):  
Amino Acids ◽  
Molecular Weight ◽  
Ferric Iron ◽  
Test Organism ◽  
The Other ◽  
Inorganic Salts ◽  
Low Molecular Weight ◽  
Straight Chain ◽  
Heat Stable ◽  
Growth Promoting

A procedure is described for the production and concentration of the 'terregens factor' (TF), a bacterial growth promoting substance synthesized by Arthrobacter pascens and essential for the growth of Arthrobacter terregens. From culture filtrates of A. pascens cultivated in a medium of inorganic salts and sucrose, concentrates of TF may be obtained that are active at 0.001 μgm. Per ml., heat stable and contain about 12.7% nitrogen. Acid hydrolysis yielded a number of amino acids, including glutamic acid, glycine, α–alanine, valine, leucine, proline, lysine, and arginine, as well as some unidentified compounds; however, TF does not appear to be a low molecular weight straight chain peptide.Although TF contains no iron, it combines readily with ferrous or ferric iron to form reddish-brown complexes with this metal. Activity for A. terregens is shown by certain iron containing complexes as hemin, coprogen, and ferrichrome. On the other hand none is shown by cytochrome or pulcherrimin; however, aspergillic acid, structurally related to the latter, possesses some growth promoting activity for the test organism.

scholarly journals Rabbit Tamm–Horsfall urinary glycoprotein. Chemical composition and subunit structure

1971 ◽  
Vol 122 (5) ◽  
pp. 623-631 ◽  
Author(s):  
Anne M. S. Marr ◽  
A. Neuberger ◽  
Wendy A. Ratcliffe
Keyword(s):  
Amino Acids ◽  
Molecular Weight ◽  
Chemical Composition ◽  
Sodium Dodecyl Sulphate ◽  
Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Gel Filtration ◽  
Cross Reactivity ◽  
Subunit Structure ◽  
Terminal Amino

1. Tamm–Horsfall glycoprotein from rabbit urine has been isolated and characterized. The homogeneity of the preparation has been established by a variety of procedures including disc gel electrophoresis and ultracentrifugation in aqueous solution, sodium dodecyl sulphate and formic acid. 2. The chemical composition has been determined and a carbohydrate content of approx. 31% was obtained. The relative contents of the amino acids were shown to be very similar to those in human Tamm–Horsfall glycoprotein. A trace of lipid was also detected. 3. Leucine was identified as the only N-terminal amino acid. 4. The subunit structure was investigated in the presence of sodium dodecyl sulphate by gel filtration and disc gel electrophoresis. These studies indicated that the subunit possessed a molecular weight of approx. 84000±6000. A similar value was obtained after reduction and S-alkylation of the glycoprotein indicating that the disulphide bonds were all intrachain. 5. A minimum value for the chemical molecular weight of 85000±6000 was obtained from the number of N-terminal amino acids released by cyanogen bromide cleavage of the glycoprotein. 6. The immunological properties of the glycoprotein were studied. Cross reactivity was demonstrated between human Tamm–Horsfall glycoprotein and a guinea-pig anti-rabbit Tamm–Horsfall antiserum.

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