A new synthesis of poly-γ-D- and L-glutamic acid

1969 ◽  
Vol 47 (19) ◽  
pp. 3690-3693 ◽  
Author(s):  
J. Kovacs ◽  
G. N. Schmit ◽  
B. J. Johnson
Keyword(s):  
Glutamic Acid ◽  
Polyglutamic Acid ◽  
New Synthesis

A new synthesis of native polyglutamic acid is described through the polycondensation of γ-glutamylglutamic acid-α,α′-di-t-butyl-γ-pentachlorophenyl ester. This route eliminates the possibility of transpeptidation.

scholarly journals A NEW SYNTHESIS OF GLUTAMIC ACID

1931 ◽  
Vol 94 (2) ◽  
pp. 599-609
Author(s):  
Max S. Dunn ◽  
B.W. Smart ◽  
C.E. Redemann ◽  
K.E. Brown
Keyword(s):  
Glutamic Acid ◽  
New Synthesis

Biosynthesis of Polyglutamic Acid and its Application on Agriculture

2011 ◽  
Vol 183-185 ◽  
pp. 1219-1223 ◽  
Author(s):  
Xiang Yu ◽  
Min Wang ◽  
Qun Hui Wang ◽  
Xu Ming Wang
Keyword(s):  
Water Treatment ◽  
Glutamic Acid ◽  
Biodegradable Polymer ◽  
Water Soluble ◽  
Future Trends ◽  
Polyglutamic Acid ◽  
Separation And Purification ◽  
Potential Applications ◽  
Purification Methods ◽  
Fermentation Parameters

Poly γ-glutamic acid (γ-PGA) is a kind of water soluble and biodegradable polymer, which is nontoxic toward humans and the environment. Therefore, the potential applications of γ-PGA and its derivatives have been of interest in a broad range such as food, cosmetics, medicine, water treatment and agriculture. This paper summarizes γ-PGA synthesis pathways in microorganisms, producing strains, fermentation parameters, as well as separation and purification methods. In addition, the prospect of γ-PGA application on agriculture was introduced, pointing out the problems and the future trends in research and application of γ-PGA.

Cerebrospinal fluid levels of alpha-synuclein measured using a poly-glutamic acid-modified gold nanoparticle-doped disposable neuro-biosensor system

The Analyst ◽  
2019 ◽  
Vol 144 (2) ◽  
pp. 611-621 ◽  
Author(s):  
Münteha Nur Sonuç Karaboğa ◽  
Mustafa Kemal Sezgintürk
Keyword(s):  
Parkinson’S Disease ◽  
Cerebrospinal Fluid ◽  
Glutamic Acid ◽  
Gold Nanoparticle ◽  
Alpha Synuclein ◽  
Polyglutamic Acid ◽  
Cerebrospinal Fluid Levels ◽  
System P ◽  
Biosensor System ◽  
Fluid Levels

A gold nanoparticle and polyglutamic acid-modified ITO-based biosensor system to detect alpha-synuclein, an important biomarker of Parkinson's disease.

scholarly journals Characterization of the Bacillus subtilis ywtD Gene, Whose Product Is Involved in γ-Polyglutamic Acid Degradation

2003 ◽  
Vol 185 (7) ◽  
pp. 2379-2382 ◽  
Author(s):  
Takao Suzuki ◽  
Yasutaka Tahara
Keyword(s):  
Escherichia Coli ◽  
Bacillus Subtilis ◽  
Glutamic Acid ◽  
Recombinant Plasmid ◽  
Signal Sequence ◽  
High Molecular Mass ◽  
Enzymatic Analysis ◽  
Polyglutamic Acid ◽  
Partial Similarity

ABSTRACT The ywtD gene, which codes for an enzyme that degrades γ-polyglutamic acid (PGA), was cloned from Bacillus subtilis IFO16449. The gene is located immediately downstream of ywsC and ywtABC, a PGA operon involved in PGA biosynthesis, and it showed partial similarity to genes coding for dl-endopeptidase, a peptidoglycan-degrading enzyme. The ywtD gene, from which signal sequence is excised, was inserted into pET15b, and the recombinant plasmid was then transformed into Escherichia coli. Histidine-tagged YwtD was purified from sonicated cells of the transformant. The purified YwtD degraded PGA to yield two hydrolyzed products, a high-molecular-mass product (490 kDa with nearly 100% l-glutamic acid) and an 11-kDa product (with d-glutamic acid and l-glutamic acid in an 80:20 ratio). This finding and results of enzymatic analysis of the two products with carboxypeptidase G suggest that YwtD is a novel enzyme cleaving the γ-glutamyl bond only between d- and l-glutamic acids of PGA, and it may be designated γ-dl-glutamyl hydrolase.

scholarly journals GENETIC CONTROL OF THE ANTIBODY RESPONSE

1967 ◽  
Vol 126 (5) ◽  
pp. 969-978 ◽  
Author(s):  
Hugh O. McDevitt ◽  
Michael Sela
Keyword(s):  
Immune Response ◽  
Antibody Response ◽  
Glutamic Acid ◽  
Genetic Control ◽  
Antigenic Determinants ◽  
Polyglutamic Acid ◽  
Cross Reactions ◽  
Cba Mice ◽  
Related Series ◽  
Synthetic Polypeptide

CBA and C57 mice were tested for their ability to make an immune response to a related series of branched, multichain synthetic polypeptide antigens in which the antigenic determinants on the amino termini of the branched side chains were systematically varied. Neither strain responded to the polyglutamic acid determinant. Both strains responded well and equally to the poly(phenylalanine, glutamic acid) determinants. CBA mice responded poorly, and C57 mice responded well to two different antigens bearing poly(tyrosine, glutamic acid) determinants. CBA mice responded well, and CS7 mice responded poorly to two different antigens bearing poly(histidine, glutamic acid) determinants. The genetic control of the immune response to (H,G)-A--L appears to be dominant and polygenic, as it has been shown to be for (T,G)-A--L. The related antigens used in this study show extensive cross-reactions with antisera against other members of the related series.

New synthesis of N-[4-[[(2-amino-4(3H)-oxopyrido[3,2-d]pyrimidin-6-yl)methyl]amino]benzoyl]-L-glutamic acid (8-deazafolic acid) and the preparation of some 5,6,7,8-tetrahydro derivatives

1981 ◽  
Vol 24 (10) ◽  
pp. 1254-1258 ◽  
Author(s):  
Carroll Temple ◽  
C. L. Kussner ◽  
J. D. Rose ◽  
D. L. Smithers ◽  
L. L. Bennett ◽  
...  
Keyword(s):  
Glutamic Acid ◽  
New Synthesis

A CONVENIENT SYNTHESIS OF DL-GLUTAMIC ACID FROM β-PROPIOLACTONE

1956 ◽  
Vol 34 (10) ◽  
pp. 1440-1443 ◽  
Author(s):  
Guy Talbot ◽  
Roger Gaudry ◽  
Louis Berlinguet
Keyword(s):  
Glutamic Acid ◽  
Acid Hydrolysis ◽  
Sodium Salt ◽  
Intermediate Product ◽  
Diethyl Ester ◽  
New Synthesis ◽  
Convenient Synthesis

A new synthesis of DL-glutamic acid was carried out in an over-all yield of 87% from condensation between β-propiolactone and the sodium salt of diethyl acetamidomalonate, followed by acid hydrolysis. When desired, the intermediate product, the diethyl ester of N-acetyl-2-carbethoxyglutamic acid, could be isolated in a 68% yield and hydrolyzed to glutamic acid via the hydrochloride in a 95% yield.

scholarly journals Poly-γ-Glutamate Capsule-Degrading Enzyme Treatment Enhances Phagocytosis and Killing of Encapsulated Bacillus anthracis

2006 ◽  
Vol 51 (1) ◽  
pp. 215-222 ◽  
Author(s):  
Angelo Scorpio ◽  
Donald J. Chabot ◽  
William A. Day ◽  
David K. O'Brien ◽  
Nicholas J. Vietri ◽  
...  
Keyword(s):  
Bacillus Subtilis ◽  
Glutamic Acid ◽  
Bacillus Anthracis ◽  
Enzyme Treatment ◽  
Human Neutrophils ◽  
Acid Hydrolase ◽  
Polyglutamic Acid ◽  
New Approach ◽  
Macrophage Phagocytosis ◽  
Phagocytic Killing

ABSTRACT The poly-γ-d-glutamic acid capsule confers antiphagocytic properties on Bacillus anthracis and is essential for virulence. In this study, we showed that CapD, a γ-polyglutamic acid depolymerase encoded on the B. anthracis capsule plasmid, degraded purified capsule and removed the capsule from the surface of anthrax bacilli. Treatment with CapD induced macrophage phagocytosis of encapsulated B. anthracis and enabled human neutrophils to kill encapsulated organisms. A second glutamylase, PghP, a γ-polyglutamic acid hydrolase encoded by Bacillus subtilis bacteriophage ΦNIT1, had minimal activity in degrading B. anthracis capsule, no effect on macrophage phagocytosis, and only minimal enhancement of neutrophil killing. Thus, the levels of both phagocytosis and killing corresponded to the degree of enzyme-mediated capsule degradation. The use of enzymes to degrade the capsule and enable phagocytic killing of B. anthracis offers a new approach to the therapy of anthrax.

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