Biosynthesis of chloramphenicol in Streptomyces species 3022a: the nature of the arylamine synthetase system

1979 ◽  
Vol 25 (12) ◽  
pp. 1408-1415 ◽  
Author(s):  
M. M. Francis ◽  
D. W. S. Westlake
Keyword(s):  
Molecular Weight ◽  
Infrared Spectrum ◽  
Pyridoxal Phosphate ◽  
Core Protein ◽  
Deae Cellulose ◽  
The Other ◽  
Small Molecular Weight ◽  
Streptomyces Species ◽  
Effector Molecules ◽  
Chorismic Acid

The arylamine synthetase which catalyses the conversion of chorismic acid to p-aminophenylalanine in Streptomyces species 3022a was separated from aminotransferase by DEAE-cellulose chromatography. Recovered activity was stimulated by the addition of the aminotransferase and pyridoxal phosphate. Activity was further fragmented into three separate components by passage through a Sephadex G-100 column. Only one component produced p-aminophenylalanine but in combination the three stimulated each other's activity. Although the products of the other two components were unstable, an infrared spectrum of one of them was obtained and confirmed the presence of an aromatic amine, but other functional groups could not be ascertained. This product was not recognized as a substrate by the arylamine synthetase complex and it was suggested that it may be a degradation product of an intermediate of p-aminophenylalanine biosynthesis or an unknown intermediate of later biosynthetic steps of the chloramphenicol pathway. It is further suggested that arylamine compounds produced by this organism are the result of interaction of a core protein with other macromolecules and small molecular weight effector molecules.

A GENERAL METHOD FOR THE ISOLATION AND PURIFICATION OF PHOSVITIN FROM VERTEBRATE EGGS

1966 ◽  
Vol 44 (12) ◽  
pp. 1647-1655 ◽  
Author(s):  
R. A. Wallace ◽  
D. W. Jared ◽  
A. Z. Eisen
Keyword(s):  
Molecular Weight ◽  
Ammonium Sulfate ◽  
Deae Cellulose ◽  
The Other ◽  
Chemical Analyses ◽  
Ammonium Sulfate Precipitation ◽  
Isolation And Purification ◽  
Complex Ii ◽  
Vertebrate Eggs ◽  
General Method

A general method has been developed for the isolation and purification of phosvitin from vertebrate eggs. The method is detailed in three steps consisting of (i) isolation of a phosvitin–lipovitellin complex; (ii) ammonium sulfate precipitation of the lipovitellin; and (iii) DEAE-cellulose chromatography of the remaining phosvitin. Phosvitin was isolated from the eggs of five representative vertebrates (lamprey, trout, frog, turtle, and chicken), and chemical analyses together with sedimentation studies were performed on the samples. Preparations were obtained with the lowest N/P ratios reported to date. The analytical results also suggested that trout phosvitin has approximately half the molecular weight (24,000) of the other proteins and that "purified" phosvitin may still be heterogeneous.

scholarly journals The xylanase system of Coniophora cerebella

1968 ◽  
Vol 108 (4) ◽  
pp. 571-576 ◽  
Author(s):  
N. J. King ◽  
D. B. Fuller
Keyword(s):  
Molecular Weight ◽  
Culture Filtrate ◽  
Uronic Acid ◽  
Enzyme System ◽  
Gel Filtration ◽  
Deae Cellulose ◽  
The Other ◽  
Xylose Residue ◽  
Random Manner ◽  
Acidic Sugars

1. The culture filtrate of the fungus Coniophora cerebella grown on poplar 4-O-methylglucuronoxylan as carbon source and enzyme inducer contained an enzyme system that degraded the polysaccharide to xylose, acidic and neutral oligosaccharides and an enzyme-resistant polymer. Free uronic acid was not produced. 2. Cold ethanol fractionation of the culture filtrate yielded two active fractions, one of which had only xylanase (EC 3.2.1.8) and the other both xylanase and xylosidase (EC 3.2.1.37) activities. Further fractionation on DEAE-cellulose resolved the xylanase and xylosidase activities. 3. The xylanase degraded poplar 4-O-methylglucuronoxylan in an essentially random manner, producing oligosaccharides, but some xylose residues in the vicinity of uronic acid side groups were protected from hydrolysis, preventing a truly random attack. The xylosidase attacked the polysaccharide very slowly, releasing xylose, but the oligosaccharides produced by the action of the xylanase were much more susceptible to hydrolysis by the xylosidase. 4. The products of xylanase action were separated into neutral and acidic fractions. The neutral oligosaccharides were separated by chromatography on charcoal–Celite, and the major products were characterized as xylobiose, xylotriose, xylotetraose and xylopentaose. Some of the acidic sugars were branched, having the uronic acid residue attached to a xylose residue other than the terminal non-reducing one. 5. Gel filtration of various xylanase fractions gave values for the molecular weight of the enzyme from 34000 to 38000.

scholarly journals The multiple forms of α-D-mannosidase in human plasma

1979 ◽  
Vol 179 (3) ◽  
pp. 583-592 ◽  
Author(s):  
S Hirani ◽  
B Winchester
Keyword(s):  
Molecular Weight ◽  
Human Plasma ◽  
Concanavalin A ◽  
Gel Filtration ◽  
Deae Cellulose ◽  
Exchange Chromatography ◽  
The Other ◽  
Multiple Forms ◽  
Simple Correlation ◽  
Multiple Components

The acidic alpha-D-mannosidase in human plasma closely resembles liver acidic alpha-D-mannosidase in its affinity for concanavalin A-Sepharose, molecular weight and resolution into multiple components on DEAE-cellulose. A combination of chromatography on concanavalin A-Sepharose and gel filtration on Sephadex G-200 and Sepharose 6B suggests that four forms of intermediate alpha-D-mannosidase, which differ either in their molecular weight of affinity for concanavalin A, exist in human plasma. A practical classification and nomenclature for the multiple forms of intermediate alpha-D-mannosidase in plasma based on molecular weight and affinity for concanavalin A is proposed. Multiple forms of intermediate alpha-D-mannosidase were also observed by ion-exchange chromatography on DEAE-cellulose, but there was not a simple correlation between these forms and those obtained with the other separation procedures. The form of intermediate alpha-D-mannosidase least abundant in plasma, approx. 7% of the activity, has very similar properties to the neutral alpha-D-mannosidase in human liver. In contrast, the other three forms of intermediate alpha-D-mannosidase, which account for over 90% of the activity, do not appear to be present in liver, except perhaps in trace amounts.

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.

Hemostatically potent small molecular weight serine protease from Maclura spinosa (Roxb. ex Willd.) accelerates healing of subcutaneous dermal wounds in Swiss albino mice

Biologia ◽  
2019 ◽  
Vol 75 (1) ◽  
pp. 139-149
Author(s):  
Venkatesh Bommalapura Kulkarni ◽  
Raghu Ram Achar ◽  
Maheshwari Mahadevappa ◽  
Dinesh Sosalagere Manjegowda ◽  
Priya Babu Shubha ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Serine Protease ◽  
Small Molecular Weight ◽  
Swiss Albino Mice ◽  
Albino Mice

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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