scholarly journals Navy (haricot)-bean (Phaseolus vulgaris) lectin. Isolation and characterization of two components from a toxic agglutinating extract

1974 ◽  
Vol 139 (2) ◽  
pp. 421-429 ◽  
Author(s):  
A. T. Andrews
Keyword(s):  
Amino Acids ◽  
Phaseolus Vulgaris ◽  
Aspartic Acid ◽  
Polypeptide Chain ◽  
Isolation And Characterization ◽  
Tetrameric Structure ◽  
A Subunit ◽  
Terminal Amino ◽  
Protein Components

Two protein components were isolated in a highly purified state from a toxic fraction from the navy (haricot) bean (Phaseolus vulgaris). One, a lectin, strongly agglutinated horse erythrocytes and leucocytes, agglutination being readily observable with both types of cell at a lectin concentration of 4μg/ml. The other component (component 1), although possessing some similarity in composition, was thought to be non-agglutinating or, at most, only very weakly so. Component 1 had a mol.wt. of about 143000 and a subunit mol.wt. of about 37000, suggesting a tetrameric structure probably with identical subunits. Alanine was the only N-terminal amino acid identified and the molecule was notable in being devoid of tryptophan and cysteine, low in methionine and high in leucine, glutamic acid and aspartic acid. The lectin was somewhat smaller (mol.wt. about 114000) and apparently also composed of four identical subunits of mol.wt. about 30000. Dansylation showed that arginine occupied the N-terminus of the polypeptide chain. Aspartic acid, serine, threonine and leucine were the predominant amino acids of the lectin, and the sulphur-containing amino acids were entirely absent. Both constituents were glycoproteins and the compositions of the carbohydrate portions (4.9% for component 1 and 8.1% for the lectin) were generally similar, consisting of mannose and glucosamine with smaller amounts of glucose and traces of xylose and arabinose.

Post-proline endopeptidase, further characterization of the enzyme from pig kidneys

1984 ◽  
Vol 49 (8) ◽  
pp. 1846-1853 ◽  
Author(s):  
Karel Hauzer ◽  
Tomislav Barth ◽  
Linda Servítová ◽  
Karel Jošt
Keyword(s):  
Amino Acids ◽  
Aspartic Acid ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Relative Molecular Mass ◽  
Enzyme Molecule ◽  
Thiol Compounds ◽  
Modified Method ◽  
N Terminus

A post-proline endopeptidase (EC 3.4.21.26) was isolated from pig kidneys using a modified method described earlier. The enzyme was further purified by ion exchange chromatography on DEAE-Sephacel. The final product contained about 95% of post-proline endopeptidase. The enzyme molecule consisted of one peptide chain with a relative molecular mass of 65 600 to 70 000, containing a large proportion of acidic and alifatic amino acids (glutamic acid, aspartic acid and leucine) and the N-terminus was formed by aspartic acid or asparagine. In order to prevent losses of enzyme activity, thiol compounds has to be added.

Purification and partial amino acid sequence of thuricin S, a new anti-Listeriabacteriocin from Bacillus thuringiensis

2007 ◽  
Vol 53 (2) ◽  
pp. 284-290 ◽  
Author(s):  
Sonia Chehimi ◽  
François Delalande ◽  
Sophie Sablé ◽  
Mohamed-Rabeh Hajlaoui ◽  
Alain Van Dorsselaer ◽  
...  
Keyword(s):  
Bacillus Thuringiensis ◽  
Proteinase K ◽  
Terminal Sequence ◽  
Partial Amino Acid Sequence ◽  
Ph Values ◽  
Heat Stable ◽  
Isolation And Characterization ◽  
Terminal Amino ◽  
Edman Sequencing

We report the isolation and characterization of a new bacteriocin, thuricin S, produced by the Bacillus thuringiensis subsp. entomocidus HD198 strain. This antibacterial activity is sensitive to proteinase K, is heat-stable, and is stable at a variety of pH values (3–10.5). The monoisotopic mass of thuricin S purified by high perfomance liquid chromatography, as determined with mass spectrometry ESI-TOF-MS, is 3137.61 Da. Edman sequencing and NanoESI-MS/MS experiments provided the sequence of the 18 N-terminal amino acids. Interestingly, thuricin S has the same N-terminal sequence (DWTXWSXL) as bacthuricin F4 and thuricin 17, produced by B. thuringiensis strains BUPM4 and NEB17, respectively, and could therefore be classified as a new subclass IId bacteriocin.

Synthesis and characterization of poly(aspartic acid) derivatives conjugated with various amino acids

2010 ◽  
Vol 18 (5) ◽  
pp. 881-890 ◽  
Author(s):  
Ji-Heung Kim ◽  
Chang Mo Son ◽  
Young Sil Jeon ◽  
Woo-Seok Choe
Keyword(s):  
Amino Acids ◽  
Aspartic Acid ◽  
Synthesis And Characterization

Isolation and characterization of new efficient and competitive bean (Phaseolus vulgaris L.) rhizobia from Brazil

2000 ◽  
Vol 32 (11-12) ◽  
pp. 1515-1528 ◽  
Author(s):  
Mariangela Hungria ◽  
Diva de S Andrade ◽  
Lígia Maria de O Chueire ◽  
Agustin Probanza ◽  
Francisco J Guttierrez-Mañero ◽  
...  
Keyword(s):  
Phaseolus Vulgaris ◽  
Phaseolus Vulgaris L ◽  
Isolation And Characterization

scholarly journals Isolation and Characterization of the Gene Coding for the Amidinotransferase Involved in the Biosynthesis of Phaseolotoxin in Pseudomonas syringae pv. phaseolicola

2001 ◽  
Vol 14 (4) ◽  
pp. 545-554 ◽  
Author(s):  
Gustavo Hernández-Guzmán ◽  
Ariel Alvarez-Morales
Keyword(s):  
Aspartic Acid ◽  
Pseudomonas Syringae ◽  
Sequence Similarity ◽  
Insertion Mutant ◽  
Halo Blight ◽  
Streptomyces Spp ◽  
Isolation And Characterization ◽  
Gene Coding ◽  
Blight Disease

Pseudomonas syringae pv. phaseolicola is the causal agent of the “halo blight” disease of beans. A key component in the development of the disease is a nonhost-specific toxin, Nδ-(N'-sulphodiaminophosphinyl)-ornithyl-alanyl-homoarginine, known as phaseolotoxin. The homoarginine residue in this molecule has been suggested to be the product of Larginine:lysine amidinotransferase activity, previously detected in extracts of P. syringae pv. phaseolicola grown under conditions of phaseolotoxin production. We report the isolation and characterization of an amidinotransferase gene (amtA) from P. syringae pv. phaseolicola coding for a polypeptide of 362 residues (41.36 kDa) and showing approximately 40% sequence similarity to Larginine:inosamine-phosphate amidinotransferase from three species of Streptomyces spp. and 50.4% with an Larginine:glycine amidinotransferase from human mitochondria. The cysteine, histidine, and aspartic acid residues involved in substrate binding are conserved. Furthermore, expression of the amtA and argK genes and phaseolotoxin production occurs at 18°C but not at 28°C. An amidinotransferase insertion mutant was obtained that lost the capacity to synthesize homoarginine and phaseolotoxin. These results show that the amtA gene isolated is responsible for the amidinotransferase activity detected previously and that phaseolotoxin production depends upon the activity of this gene.

scholarly journals Isolation and Characterization of Mutations in theEscherichia coli Regulatory Protein XapR

1999 ◽  
Vol 181 (14) ◽  
pp. 4397-4403 ◽  
Author(s):  
Casper Jørgensen ◽  
Gert Dandanell
Keyword(s):  
Amino Acids ◽  
Purine Nucleoside Phosphorylase ◽  
Mutational Analysis ◽  
Regulatory Protein ◽  
Three Dimensional ◽  
Dimensional Structure ◽  
Wild Type ◽  
Isolation And Characterization ◽  
In The Wild

ABSTRACT In this work, the LysR-type protein XapR has been subjected to a mutational analysis. XapR regulates the expression of xanthosine phosphorylase (XapA), a purine nucleoside phosphorylase inEscherichia coli. In the wild type, full expression of XapA requires both a functional XapR protein and the inducer xanthosine. Here we show that deoxyinosine can also function as an inducer in the wild type, although not to the same extent as xanthosine. We have isolated and characterized in detail the mutants that can be induced by other nucleosides as well as xanthosine. Sequencing of the mutants has revealed that two regions in XapR are important for correct interactions between the inducer and XapR. One region is defined by amino acids 104 and 132, and the other region, containing most of the isolated mutations, is found between amino acids 203 and 210. These regions, when modelled into the three-dimensional structure of CysB from Klebsiella aerogenes, are placed close together and are most probably directly involved in binding the inducer xanthosine.

ISOLATION AND CHARACTERIZATION OF RIBONUCLEIC ACID FROM RAT LENS

1962 ◽  
Vol 40 (1) ◽  
pp. 41-47 ◽  
Author(s):  
Anima Devi
Keyword(s):  
Amino Acids ◽  
The Other ◽  
Ocular Lens ◽  
E Coli ◽  
Isolation And Characterization ◽  
Coiled Structure ◽  
Calf Thymus ◽  
Original Procedure ◽  
Polynucleotide Chain

RNA from rat ocular lens has been isolated by a method based on Kirby's original procedure (7), but greatly modified so as to avoid any degradation of RNA by RNase during the process of its extraction from lenses. The absorption at 260 mμ of a 1.0% solution of this purified material in a 1-cm cell is 1.95. Its N/P ratio is 1.58. It has 20 to 25% activity of that of yeast-soluble RNA in accepting activated amino acids. When this RNA (like all other RNA's) is heated and cooled the polynucleotide chain can again form loops, thus suggesting a randomly coiled structure for this RNA. On the other hand, DNA preparations from calf thymus, rat liver, and E. coli showed irreversible changes when heated and cooled.

Isolation and characterization of the fission yeast gene rpa42 +, which encodes a subunit shared by RNA polymerases I and III

1999 ◽  
Vol 262 (4-5) ◽  
pp. 749-757 ◽  
Author(s):  
Y. Imazawa ◽  
K. Imai ◽  
A. Fukushima ◽  
K. Hisatake ◽  
M. Muramatsu ◽  
...  
Keyword(s):  
Fission Yeast ◽  
Rna Polymerases ◽  
Yeast Gene ◽  
Isolation And Characterization ◽  
A Subunit
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