Nontoxic and toxic oligopeptides with D-amino acids and unusual residues in Microcystis aeruginosa PCC 7806

1989 ◽  
Vol 151 (5) ◽  
pp. 411-415 ◽  
Author(s):  
I. M. Birk ◽  
R. Dierstein ◽  
I. Kaiser ◽  
U. Matern ◽  
W. A. König ◽  
...  
Keyword(s):  
Amino Acids ◽  
Microcystis Aeruginosa

ISOLATION AND IDENTIFICATION OF THE FAST-DEATH FACTOR IN MICROCYSTIS AERUGINOSA NRC-1

1959 ◽  
Vol 37 (1) ◽  
pp. 453-471 ◽  
Author(s):  
C. T. Bishop ◽  
E. F. L. J. Anet ◽  
P. R. Gorham
Keyword(s):  
Amino Acids ◽  
Molecular Weight ◽  
Body Weight ◽  
Microcystis Aeruginosa ◽  
Sodium Salt ◽  
Cyclic Peptide ◽  
Isolation And Identification ◽  
Toxic Compound ◽  
Molar Ratios ◽  
Crude Preparation

The fast-death factor in Microcystis aeruginosa NRC-1 is an acidic, probably cyclic peptide containing the following amino acids in the molar ratios indicated: L-aspartic (1); L-glutamic (2); D-serine (1); L-valine (1); L-ornithine (1); L-alanine (2); L-leucine (2). It is possible, although not likely, that one of the residues of glutamic, alanine, or leucine also is in the D-configuration. The toxin, in the form of its sodium salt, was extracted from lyophilized algal cells by water, separated from pigments by extraction into n-butanol, and freed from high-molecular-weight impurities by dialysis. No separation of a single toxic compound could be obtained by countercurrent distribution, chromatography, or electrophoresis in carbonate, acetate, or phosphate buffers. Electrophoresis of the crude toxin on cellulose in 0.1 M borate yielded five peptides one of which was toxic and accounted for 100% of the toxicity present in the crude preparation. The intraperitoneal LD50of the pure toxin for mice was 0.466 ± 0.013 mg/kg body weight.

scholarly journals A formal synthesis of Balgacyclamide A using solution phase fragments condensation.

2020 ◽  
Author(s):  
Sandip Radhakisan Ugale ◽  
Somnath S Gholap
Keyword(s):  
Amino Acids ◽  
Total Synthesis ◽  
Spectral Data ◽  
Microcystis Aeruginosa ◽  
Solution Phase ◽  
Formal Synthesis ◽  
H Nmr ◽  
The Core ◽  
C Nmr

Abstract: A formal total synthesis of Balgacyclamide A as an antimalarial cynobactin of Microcystis aeruginosa (EAWAG 251) has been described. The synthesis of titled cyclamide was accomplished by the solution phase fragment synthesis using protection, deprotection and macrocylization process. Four common amino acids such as d-alanine, l-threonine, l-valine and d-allo-isoleucine, has been used for the construction of Balgacyclamide A. Including, the oxazoline and thiazole are the core structures was successfully achieved by using Burgess reagent and Hantzsch methods. The overall yield of the synthesized balgacyclamide A was found to be 2.03%, also structure was confirmed by1H-NMR, 13C-NMR and HRMS spectral data.

Effects of amino acids on microcystin production of the Microcystis aeruginosa

2009 ◽  
Vol 161 (2-3) ◽  
pp. 730-736 ◽  
Author(s):  
Ruihua Dai ◽  
Huijuan Liu ◽  
Jiuhui Qu ◽  
Xu Zhao ◽  
Yining Hou
Keyword(s):  
Amino Acids ◽  
Microcystis Aeruginosa ◽  
Microcystin Production

ISOLATION AND IDENTIFICATION OF THE FAST-DEATH FACTOR IN MICROCYSTIS AERUGINOSA NRC-1

1959 ◽  
Vol 37 (3) ◽  
pp. 453-471 ◽  
Author(s):  
C. T. Bishop ◽  
E. F. L. J. Anet ◽  
P. R. Gorham
Keyword(s):  
Amino Acids ◽  
Molecular Weight ◽  
Body Weight ◽  
Microcystis Aeruginosa ◽  
Sodium Salt ◽  
Cyclic Peptide ◽  
Isolation And Identification ◽  
Toxic Compound ◽  
Molar Ratios ◽  
Crude Preparation

The fast-death factor in Microcystis aeruginosa NRC-1 is an acidic, probably cyclic peptide containing the following amino acids in the molar ratios indicated: L-aspartic (1); L-glutamic (2); D-serine (1); L-valine (1); L-ornithine (1); L-alanine (2); L-leucine (2). It is possible, although not likely, that one of the residues of glutamic, alanine, or leucine also is in the D-configuration. The toxin, in the form of its sodium salt, was extracted from lyophilized algal cells by water, separated from pigments by extraction into n-butanol, and freed from high-molecular-weight impurities by dialysis. No separation of a single toxic compound could be obtained by countercurrent distribution, chromatography, or electrophoresis in carbonate, acetate, or phosphate buffers. Electrophoresis of the crude toxin on cellulose in 0.1 M borate yielded five peptides one of which was toxic and accounted for 100% of the toxicity present in the crude preparation. The intraperitoneal LD50of the pure toxin for mice was 0.466 ± 0.013 mg/kg body weight.

Removal efficiency of MIEX® pretreatment on typical proteins and amino acids derived from Microcystis aeruginosa

RSC Advances ◽  
2016 ◽  
Vol 6 (65) ◽  
pp. 60869-60876 ◽  
Author(s):  
Cheng Liu ◽  
Siyuan He ◽  
Zhehao Sun ◽  
Jie Wang ◽  
Wei Chen
Keyword(s):  
Amino Acids ◽  
Microcystis Aeruginosa ◽  
Removal Efficiency

Main categories of typical proteins and amino acids derived fromM. aeruginosawere identified and their removal by MIEX® was discussed.

A new isolation and structure for the endotoxin from Microcystis aeruginosa NRC-1

1970 ◽  
Vol 48 (4) ◽  
pp. 508-510 ◽  
Author(s):  
J. Rama Murthy ◽  
J. B. Capindale
Keyword(s):  
Amino Acids ◽  
Body Weight ◽  
Solvent Extraction ◽  
Microcystis Aeruginosa ◽  
Green Alga ◽  
Complex Structure ◽  
Strain Analysis ◽  
Blue Green Alga ◽  
Algal Strain ◽  
Toxic Material

The endotoxin from the blue–green alga Microcystis aeruginosa NRC-1 has been isolated as its ammonium salt by a new procedure involving solvent extraction and elution from DEAE-Sephadex A-25. The intraperitoneal LD100 of this toxin preparation for mice was 0.1 mg/kg body weight. The product is a white solid which appears to be chromatographically and electrophoretically homogeneous. This toxin produces similar symptoms in mice to those described originally for the toxic material from the same algal strain. Analysis of the toxin hydrolysate indicates a more complex structure since seven more amino acids have been found, including tyrosine, proline, and arginine, in addition to the seven reported before.

Homochirality as the Signature of Extra-Terrestrial Life

1997 ◽  
Vol 161 ◽  
pp. 505-510
Author(s):  
Alexandra J. MacDermott ◽  
Laurence D. Barron ◽  
Andrè Brack ◽  
Thomas Buhse ◽  
John R. Cronin ◽  
...  
Keyword(s):  
Amino Acids ◽  
Protein Synthesis ◽  
Optical Rotation ◽  
Physical Origin ◽  
Natural Choice ◽  
Rosetta Mission ◽  
Terrestrial Life ◽  
Subsurface Layers ◽  
Solar System Bodies ◽  
Origin Of Homochirality

AbstractThe most characteristic hallmark of life is its homochirality: all biomolecules are usually of one hand, e.g. on Earth life uses only L-amino acids for protein synthesis and not their D mirror images. We therefore suggest that a search for extra-terrestrial life can be approached as a Search for Extra- Terrestrial Homochirality (SETH). The natural choice for a SETH instrument is optical rotation, and we describe a novel miniaturized space polarimeter, called the SETH Cigar, which could be used to detect optical rotation as the homochiral signature of life on other planets. Moving parts are avoided by replacing the normal rotating polarizer by multiple fixed polarizers at different angles as in the eye of the bee. We believe that homochirality may be found in the subsurface layers on Mars as a relic of extinct life, and on other solar system bodies as a sign of advanced pre-biotic chemistry. We discuss the chiral GC-MS planned for the Roland lander of the Rosetta mission to a comet and conclude with theories of the physical origin of homochirality.

Sign in / Sign up

Export Citation Format

Share Document