Induction et repression de la synthèse de collagénase chez Acinetobacter sp.

1979 ◽  
Vol 25 (5) ◽  
pp. 611-617 ◽  
Author(s):  
Jean-Claude Monboisse ◽  
Jean Labadie ◽  
Philippe Gouet
Keyword(s):  
Amino Acids ◽  
Molecular Weight ◽  
Catabolite Repression ◽  
Tertiary Structure ◽  
Protein Hydrolysate ◽  
The Other ◽  
Similar Composition ◽  
Acid Hydrolysate ◽  
Acinetobacter Sp ◽  
Casamino Acids

The synthesis of collagenase in Acinetobacter sp. was found to be inducible by denatured collagen and by its high molecular weight fragments. The presence in the inducer of part of the tertiary structure appear to be indispensable. On the other hand, an addition of Casamino acids, meat protein hydrolysate, or a mixture of amino acids with a similar composition to gelatin does not stimulate collagenase synthesis.Enzyme production was severely repressed in the early phase of growth by glucose, arabinose, and ribose, single amino acids, proline, hydroxyproline, alanine, glutamic acid, or casein acid hydrolysate. A mechanism of repression similar to catabolite repression was involved in the phenomenon caused by carbohydrates. However, the fact that cyclic adenosine 3′5′-mono-phosphate did not overcome the repression caused by amino acids or Casamino acids, in contrast to classical catabolite repression, suggests that these two forms of repression may be distinct. [Traduit par le journal]

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.

Low Molecular Weight Sunflower Protein Hydrolysate with Low Concentration in Aromatic Amino Acids

1996 ◽  
Vol 44 (4) ◽  
pp. 967-971 ◽  
Author(s):  
Juan Bautista ◽  
Inmaculada Hernandez-Pinzon ◽  
Manuel Alaiz ◽  
Juan Parrado ◽  
Francisco Millan
Keyword(s):  
Amino Acids ◽  
Molecular Weight ◽  
Protein Hydrolysate ◽  
Aromatic Amino Acids ◽  
Low Molecular Weight ◽  
Low Concentration ◽  
Sunflower Protein

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

1954 ◽  
Vol 32 (4) ◽  
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 Studies in peroxidase action I —The oxidation of aniline

1935 ◽  
Vol 119 (812) ◽  
pp. 47-60 ◽  
Keyword(s):  
Amino Acids ◽  
Fatty Acids ◽  
Molecular Weight ◽  
Phenolic Compounds ◽  
Wide Distribution ◽  
The Other ◽  
Metabolic Processes ◽  
Inherent Property ◽  
Biological Importance ◽  
Phenylene Diamine

The production of colours by the action of the enzyme peroxidase on various amino and phenolic compounds has been recorded from time to time, but such reactions have, in general, been regarded merely as tests for the presence of peroxidase, and the nature of the coloured products has been determined only in a few instances. The fairly wide distribution of the enzyme, more particularly in plants, suggests that it has considerable biological importance, but the role that it plays in metabolic processes has not yet been elucidated. From the work of Elliott (1932, a, b ), it would appear that the enzyme is not concerned with general oxidative katabolism since it does not attack the majority of amino-acids, fatty acids, and carbohydrates. On the other hand, where the products of oxidation have been investigated, they have proved to be, in general, of higher molecular weight than the substrate. Thus, for example, guaiacol is oxidized to tetraguaiacol (Bertrand, 1903), pyrogallol to purpurogallin (Willstätter and Heiss, 1923), and o -phenylene diamine to 2:3-diamino-diphenazine (Chodat, 1925). It may well be an inherent property of the molecule which is causing condensation in the above cases, and it does not therefore necessarily follow that the enzyme is facilitating coupling of the substrate molecules as well as causing oxidation.

The Kidney and Fibrinolysis

1970 ◽  
Vol 24 (01/02) ◽  
pp. 026-032 ◽  
Author(s):  
N. A Marsh
Keyword(s):  
Molecular Weight ◽  
Plasminogen Activator ◽  
Enzyme System ◽  
Normal Animal ◽  
Fibrinolytic Enzyme ◽  
The Other ◽  
Exclusion Chromatography ◽  
Normal Urine ◽  
Renal Origin ◽  
Molecular Exclusion Chromatography

SummaryMolecular exclusion chromatography was performed on samples of urine from normal and aminonucleoside nephrotic rats. Normal urine contained 2 peaks of urokinase activity, one having a molecular weight of 22,000 and the other around 200,000. Nephrotic urine contained three peaks of activity with MW’s 126,000, 60,000 and 30,000. Plasma activator determined from euglobulin precipitate had a MW. in excess of 200,000. The results indicate that in the normal animal, plasma plasminogen activator does not escape into the urine in substantial quantities but under the conditions of extreme proteinuria there may be some loss through the kidney. The alteration in urokinase output in nephrotic animals indicates a greatly disordered renal fibrinolytic enzyme system.The findings of this study largely support the hypothesis that plasma plasminogen activator of renal origin and urinary plasminogen activator (urokinase) are different molecular species.

Rapid Isolation of High Molecular Weight Urokinase from Native Human Urine

1982 ◽  
Vol 47 (03) ◽  
pp. 197-202 ◽  
Author(s):  
Kurt Huber ◽  
Johannes Kirchheimer ◽  
Bernd R Binder
Keyword(s):  
Molecular Weight ◽  
High Molecular Weight ◽  
Human Urine ◽  
Gel Filtration ◽  
Chain Structure ◽  
The Other ◽  
Single Chain ◽  
Apparent Homogeneity ◽  
Sequential Adsorption

SummaryUrokinase (UK) could be purified to apparent homogeneity starting from crude urine by sequential adsorption and elution of the enzyme to gelatine-Sepharose and agmatine-Sepharose followed by gel filtration on Sephadex G-150. The purified product exhibited characteristics of the high molecular weight urokinase (HMW-UK) but did contain two distinct entities, one of which exhibited a two chain structure as reported for the HMW-UK while the other one exhibited an apparent single chain structure. The purification described is rapid and simple and results in an enzyme with probably no major alterations. Yields are high enough to obtain purified enzymes for characterization of UK from individual donors.

Complete Covalent Structure of Human Platelet Factor 4

1979 ◽  
Vol 42 (05) ◽  
pp. 1652-1660 ◽  
Author(s):  
Francis J Morgan ◽  
Geoffrey S Begg ◽  
Colin N Chesterman
Keyword(s):  
Amino Acids ◽  
Molecular Weight ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Human Platelet ◽  
Platelet Factor 4 ◽  
Platelet Factor ◽  
Disulphide Bonds ◽  
Covalent Structure

SummaryThe amino acid sequence of the subunit of human platelet factor 4 has been determined. Human platelet factor 4 consists of identical subunits containing 70 amino acids, each with a molecular weight of 7,756. The molecule contains no methionine, phenylalanine or tryptophan. The proposed amino acid sequence of PF4 is: Glu-Ala-Glu-Glu-Asp-Gly-Asp-Leu-Gln-Cys-Leu-Cys-Val-Lys-Thr-Thr-Ser- Gln-Val-Arg-Pro-Arg-His-Ile-Thr-Ser-Leu-Glu-Val-Ile-Lys-Ala-Gly-Pro-His-Cys-Pro-Thr-Ala-Gin- Leu-Ile-Ala-Thr-Leu-Lys-Asn-Gly-Arg-Lys-Ile-Cys-Leu-Asp-Leu-Gln-Ala-Pro-Leu-Tyr-Lys-Lys- Ile-Ile-Lys-Lys-Leu-Leu-Glu-Ser. From consideration of the homology with p-thromboglobulin, disulphide bonds between residues 10 and 36 and between residues 12 and 52 can be inferred.

scholarly journals Adiponectin: Structure, Physiological Functions, Role in Diseases, and Effects of Nutrition

Nutrients ◽  
2021 ◽  
Vol 13 (4) ◽  
pp. 1180
Author(s):  
Kayvan Khoramipour ◽  
Karim Chamari ◽  
Amirhosein Ahmadi Hekmatikar ◽  
Amirhosein Ziyaiyan ◽  
Shima Taherkhani ◽  
...  
Keyword(s):  
Cardiovascular Disease ◽  
Amino Acids ◽  
Molecular Weight ◽  
Energy Regulation ◽  
Treatment Interventions ◽  
Adipose Tissues ◽  
Physiological Functions ◽  
Cellular Events ◽  
Healthy Nutrition

Adiponectin (a protein consisting of 244 amino acids and characterized by a molecular weight of 28 kDa) is a cytokine that is secreted from adipose tissues (adipokine). Available evidence suggests that adiponectin is involved in a variety of physiological functions, molecular and cellular events, including lipid metabolism, energy regulation, immune response and inflammation, and insulin sensitivity. It has a protective effect on neurons and neural stem cells. Adiponectin levels have been reported to be negatively correlated with cancer, cardiovascular disease, and diabetes, and shown to be affected (i.e., significantly increased) by proper healthy nutrition. The present review comprehensively overviews the role of adiponectin in a range of diseases, showing that it can be used as a biomarker for diagnosing these disorders as well as a target for monitoring the effectiveness of preventive and treatment interventions.

Barricyclin D1—a dimeric ellagitannin with a macrocyclic structure—and accompanying tannins from Barringtonia racemosa

2021 ◽  
Author(s):  
Shinji Yoshikawa ◽  
Lih-Geeng Chen ◽  
Morio Yoshimura ◽  
Yoshiaki Amakura ◽  
Tsutomu Hatano ◽  
...  
Keyword(s):  
Molecular Weight ◽  
High Molecular Weight ◽  
Natural Resource ◽  
The Other ◽  
Hydrolysable Tannin ◽  
The Family ◽  
Macrocyclic Structure

Abstract Our examination of high molecular weight polyphenolic constituents in the leaves of Barringtonia racemosa of the family Lecythidaceae uncovered five previously undescribed ellagitannins. One, barringtin M1 (1), among them was a hydrolysable tannin monomer, while remaining four, barringtins D1 (2), D2 (3), D3 (4) and barricyclin D1 (5), were all dimers. Barricyclin D1 had a first macrocyclic structure formed from casuarictin (6) and tellimagrandin I (7), and the other ellagitannins had structures related to 5. Two additional known phenolics, valoneic acid dilactone (8) and schimawalin A (9), were also isolated from the leaves. These results suggested that the leaves of B. racemosa is a natural resource rich in hydrolysable tannin oligomers.

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