Modification of carboxyl groups in bovine carboxypeptidase A. II. Chemical identification of a functional glutamic acid residue and other reactive groups

Biochemistry ◽  
1971 ◽  
Vol 10 (17) ◽  
pp. 3171-3177 ◽  
Author(s):  
Hans Neurath ◽  
Philip H. Petra
Keyword(s):  
Glutamic Acid ◽  
Carboxyl Groups ◽  
Chemical Identification ◽  
Carboxypeptidase A ◽  
Glutamic Acid Residue ◽  
Reactive Groups

Sequence Determination of a Protein with N-Terminal Glutamic Acid after Modification of Carboxyl Groups with Carbodiimide as the Coupling Agent

1974 ◽  
Vol 52 (6) ◽  
pp. 560-562
Author(s):  
C. Gilardeau ◽  
M. Chrétien
Keyword(s):  
Methyl Ester ◽  
Glutamic Acid ◽  
Water Soluble ◽  
Carboxyl Groups ◽  
Edman Degradation ◽  
Sequence Determination ◽  
Glutamic Acid Residue ◽  
N Terminus ◽  
Glycine Methyl Ester

Glutamine and asparagine residues in proteins can be differentiated from glutamic and aspartic residues, during the Edman degradation, after modification of the carboxyl groups by glycine methyl ester in presence of a water-soluble carbodiimide. When applied to ovine and porcine beta-lipotropic hormones, which have a glutamic acid residue at the N-terminus, the carbodiimide blocks the N-terminus. However, the Edman degradation proceeds normally, if the phenylthiocarbamyl derivative is formed prior to the modification reaction with glycine. In this communication, radioactive glycine was used to modify the carboxyl groups.

Synthesis and properties of oxytocin analogues acting as irreversible inhibitors of the uterotonic response to oxytocin

1979 ◽  
Vol 44 (8) ◽  
pp. 2573-2582 ◽  
Author(s):  
Michal Lebl ◽  
Vera Bojanovska ◽  
Tomislav Barth ◽  
Karel Jošt
Keyword(s):  
Glutamic Acid ◽  
Active Esters ◽  
Irreversible Inhibitors ◽  
Reactive Groups ◽  
Chemical Character

A series of compounds containing reactive groups of different chemical character was synthetized from [4-glutamic acid]deamino-1-carba-oxytocin or from [2-O-methyltyrosine, 4-glutamic acid]deamino-1-carba-oxytocin. The analogues acted as specific irreversible inhibitors of the uterotonic response to oxytocin. Active esters of the initial compounds were the most effective inhibitors.

scholarly journals The Identification of a Glutamic Acid Residue as Part of the Active Site of Ribonuclease T1

1967 ◽  
Vol 242 (20) ◽  
pp. 4682-4690 ◽  
Author(s):  
Kenji Takahashi ◽  
William H. Stein ◽  
Stanford Moore
Keyword(s):  
Glutamic Acid ◽  
Active Site ◽  
Ribonuclease T1 ◽  
Glutamic Acid Residue

Tu1049 Serum Des-y-Carboxy Prothrombin Ratio by Glutamic Acid Residue Is a Novel Useful Biomarker for Hepatocellular Carcinoma

2013 ◽  
Vol 144 (5) ◽  
pp. S-1040
Author(s):  
Masahiko Tameda ◽  
Katsuya Shiraki ◽  
Kazushi Sugimoto ◽  
Suguru Ogura ◽  
Yuji Inagaki ◽  
...  
Keyword(s):  
Hepatocellular Carcinoma ◽  
Glutamic Acid ◽  
Glutamic Acid Residue

scholarly journals Targeting of the transcription factor Max during apoptosis: phosphorylation-regulated cleavage by caspase-5 at an unusual glutamic acid residue in position P1

2001 ◽  
Vol 358 (3) ◽  
pp. 705 ◽  
Author(s):  
Anja KRIPPNER-HEIDENREICH ◽  
Robert V. TALANIAN ◽  
Renate SEKUL ◽  
Regine KRAFT ◽  
Hubert THOLE ◽  
...  
Keyword(s):  
Transcription Factor ◽  
Glutamic Acid ◽  
Glutamic Acid Residue

scholarly journals Coordination chemistry of glutathione.

1999 ◽  
Vol 46 (3) ◽  
pp. 567-580 ◽  
Author(s):  
A Krezel ◽  
W Bal
Keyword(s):  
Glutamic Acid ◽  
Metal Ions ◽  
Metal Ion ◽  
Reduced Glutathione ◽  
Transition Metal Ions ◽  
Oxidized Glutathione ◽  
Binding Modes ◽  
Glutamic Acid Residue ◽  
Reduced And Oxidized Glutathione ◽  
Soft Metal

The metal ion coordination abilities of reduced and oxidized glutathione are reviewed. Reduced glutathione (GSH) is a very versatile ligand, forming stable complexes with both hard and soft metal ions. Several general binding modes of GSH are described. Soft metal ions coordinate exclusively or primarily through thiol sulfur. Hard ones prefer the amino acid-like moiety of the glutamic acid residue. Several transition metal ions can additionally coordinate to the peptide nitrogen of the gamma-Glu-Cys bond. Oxidized glutathione lacks the thiol function. Nevertheless, it proves to be a surprisingly efficient ligand for a range of metal ions, coordinating them primarily through the donors of the glutamic acid residue.

scholarly journals Impact of negatively charged patches on the surface of MHC class II antigen-presenting proteins on risk of chronic beryllium disease

2007 ◽  
Vol 5 (24) ◽  
pp. 749-758 ◽  
Author(s):  
James A Snyder ◽  
Eugene Demchuk ◽  
Erin C McCanlies ◽  
Christine R Schuler ◽  
Kathleen Kreiss ◽  
...  
Keyword(s):  
Glutamic Acid ◽  
Mhc Class Ii ◽  
Protein Interactions ◽  
Class Ii ◽  
Chronic Beryllium Disease ◽  
Glutamic Acid Residue ◽  
The One ◽  
Class Ii Antigen ◽  
Antigen Presenting ◽  
Beryllium Disease

Chronic beryllium disease (CBD) is a granulomatous lung disease that occurs primarily in workers who are exposed to beryllium dust or fumes. Although exposure to beryllium is a necessary factor in the pathobiology of CBD, alleles that code for a glutamic acid residue at the 69th position of the HLA-DPβ1 gene have previously been found to be associated with CBD. To date, 43 HLA-DPβ1 alleles that code for glutamic acid 69 (E69) have been described. Whether all of these E69 coding alleles convey equal risk of CBD is unknown. The present study demonstrates that, on the one hand, E69 alleloforms of major histocompatibility complex class II antigen-presenting proteins with the greatest negative surface charge convey the highest risk of CBD, and on the other hand, irrespective of allele, they convey equal risk of beryllium sensitization (BeS). In addition, the data suggest that the same alleles that cause the greatest risk of CBD are also important for the progression from BeS to CBD. Alleles convey the highest risk code for E26 in a constant region and for E69, aspartic acid 55 (D55), E56, D84 and E85 in hypervariable regions of the HLA-DPβ1 chain. Together with the calculated high binding affinities for beryllium, these results suggest that an adverse immune response, leading to CBD, is triggered by chemically specific metal–protein interactions.

Characterization of the role of LtgB, a putative lytic transglycosylase in Neisseria gonorrhoeae

Microbiology ◽  
2005 ◽  
Vol 151 (9) ◽  
pp. 3081-3088 ◽  
Author(s):  
Petra L. Kohler ◽  
Karen A. Cloud ◽  
Kathleen T. Hackett ◽  
Eric T. Beck ◽  
Joseph P. Dillard
Keyword(s):  
Neisseria Gonorrhoeae ◽  
Glutamic Acid ◽  
Biological Activities ◽  
Point Mutations ◽  
Normal Growth ◽  
Multiple Systems ◽  
Glutamic Acid Residue ◽  
Lytic Transglycosylase ◽  
Lysis Activity ◽  
Pathogenesis Related

Neisseria gonorrhoeae releases monomeric peptidoglycan (PG) fragments during growth. These PG fragments affect pathogenesis-related phenotypes including induction of inflammatory cytokines and killing of ciliated fallopian tube cells. Although the biological activities of these molecules have been established in multiple systems, the genes and gene products responsible for their production in N. gonorrhoeae have not been determined. The authors previously identified genes for three lytic transglycosylase homologues (ltgA, ltgB and ltgC) in the N. gonorrhoeae genome sequence. Mutation of ltgA was found to affect PG fragment release, and mutation of ltgC affected cell separation. In this study the effects of complete deletion or point mutations in ltgB were characterized. Point mutations were introduced by a combination of insertion-duplication mutagenesis and positive and negative selection, thereby generating selectable marker-less mutations. The ltgB deletion mutant had normal growth characteristics and was not affected in PG fragment release. When expressed in Escherichia coli, gonococcal LtgB was able to substitute for lambda endolysin to cause cell lysis. Mutation of the predicted catalytic-site glutamic acid residue did not decrease lysis in this system. However, mutation of a nearby glutamic acid residue eliminated lysis activity.

scholarly journals The binding of hydrogen ions to an acidic glycoprotein from bovine cortical bone

1967 ◽  
Vol 105 (3) ◽  
pp. 1171-1175 ◽  
Author(s):  
A. R. Peacocke ◽  
P A Williams
Keyword(s):  
Sodium Chloride ◽  
Glutamic Acid ◽  
Titration Curve ◽  
Analytical Data ◽  
Total Content ◽  
Bone Sialoprotein ◽  
Model Systems ◽  
Carboxyl Groups ◽  
Hydrogen Ions ◽  
Titration Curves

The H+ ion dissociation of bone sialoprotein in 0·2m-sodium chloride at 25° was studied. The total content of carboxyl groups available for titration was calculated by comparing the titration curve with the titration curves of three model systems and by the use of analytical data. This comparison showed that 7·0 carboxyl groups/mol. do not participate in the titration, and it is proposed that these are aspartic acid or glutamic acid carboxyl groups present as amides; this is also indicated by titration of the sialoprotein after acid hydrolysis. The titration of carboxyl groups was found to agree well with the Linderstrøm-Lang equation for spherical macroions.

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