Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: UNIPROT:P00790 (PGA)
 2,475 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

In the course of gamma-poly (glutamic acid) gamma-PGA fermentation, metal ions K+, Mg2+, Fe3+, Ca2+, Mo6+, Mn2+, Co2+ and Zn2+ in the medium have certain effects on the synthesis of gamma-poly(glutamic acid). Excess or lack of K+, Mg2+ and Fe3+ results in reduced yield of gamma-PGA. It was found that the gamma-PGA synthesis by Bacillus licheniformis was promoted obviously by Ca2+ and Mo6+. Synthesis and stereochemical composition of gamma-PGA was greatly regulated by Mn2+. gamma-PGA was not produced without Mn2+ in medium, and with the increase of Zn2+ concentration the yield of gamma-PGA and the proportion of D-glutamic acid in the peptide increase. Regulative effect of Co2+ and Zn2+ was almost the same as that of Mn2+, thus the combination of Mn2+, Co2+ cannot enhance gamma-PGA synthesis and affect stereochemical composition of gamma-PGA. Based on the experimental date, an appropriate formulation of metal ions in the medium for gamma-PGA production was obtained.
 ...
PMID:[Effects of metal ions on gamma-poly (glutamic acid) synthesis by Bacillus licheniformis]. 1191 Jul 70

The synthesis and evaluation for anti- and proapoptotic properties of cyclopentenone prostaglandin analogs are described. Novel J-type analogs of NEPP11 with a cross-conjugated cyclopentadienone moiety and a lipophilic omega-side chain suppressed manganese ion-induced apoptosis of PC12 cells at comparable levels to NEPP11, while monoenone derivatives were inactive. The proapoptotic activities of J-type analogs were much lower than that of NEPP11. Natural 15-deoxy-Delta(12,14)-PGJ(2) and Delta(7)-PGA(1) methyl ester were highly toxic, inducing apoptosis at lower concentrations.
 ...
PMID:Synthesis of neuroprotective cyclopentenone prostaglandin analogs: suppression of manganese-induced apoptosis of PC12 cells. 1770 24

A study of the practical applications of the addition of paramagnetic spin relaxation (PSR) ions to a variety of polymers (PLL, PAA, PGA, PVP, and polysaccharides such as hyaluronic acid, chitosan, mannan, and dextran) in solution (D2O and DMSO-d6) is described. Use of Gd(III), Cu(II), and Mn(II) allows a reduction of up to 500% in the 1H longitudinal relaxation times (T1), and so in the time necessary for recording quantitative NMR spectra (sensitivity enhancement) neither an increase of the spectral line width nor chemical shift changes resulted from addition of any of the PSR agents tested. Selective suppression of the 1H and 13C NMR signals of certain components (low MW molecules and polymers) in the spectrum of a mixture was attained thanks to their different sensitivity [transverse relaxation times (T2)] to Gd(III) (PSR filter). Illustration of this strategy with block copolymers (PGA-g-PEG) and mixtures of polymers and low MW molecules (i.e., lactose-hyaluronic acid, dextran-PAA, PVP-glutamic acid) in 1D and 2D NMR experiments (COSY and HMQC) is presented. In those mixtures where PSR and CPMG filters alone failed in the suppression of certain components (i.e., PVP-mannan-hyaluronic acid) due to their similarity of 1H T2 values and sensitivities to Gd(III), use of the PSR filter in combination with CPMG sequences (PSR-CPMG filter) successfully resulted in the sequential suppression of the components (hyaluronic acid first and then mannan).
 ...
PMID:Paramagnetic NMR relaxation in polymeric matrixes: sensitivity enhancement and selective suppression of embedded species (1H and 13C PSR filter). 1800 45

3-Phosphoglycerate kinase (3-PGK) has been purified to apparent homogeneity from Ehrlich ascites carcinoma (EAC) cells by (NH4)2SO4 precipitation, gel filtration and ion-exchange chromatography. The enzyme has been partially characterized and compared with the characteristics of this enzyme of other normal and malignant cells. The EAC cell 3-PGK is composed of a single subunit of 47 kDa. It has a broad pH optimum (pH 6.0-7.5) for its enzymatic activity. The apparent Km values of 3-phosphoglycerate (3-PGA) and ATP for 3-PGK have been found out to be 0.25 mM and 0.1 mM respectively. Similar to 3-PGK of other cells, the EAC enzyme requires either Mg2+ or Mn2+ for full activity; the optimum concentrations of Mg2+ and Mn2+ are 0.8 mM and 0.5 mM respectively. When ATP and 3-PGA act as substrates, ADP, the reaction product of 3-PGK-catalyzed reaction has been found to inhibit this enzyme. Kinetic studies were made on the inhibition of ADP in presence of the substrates ATP and 3-PGA. Attempts to hybridize 3-PGK and glyceraldehyde-3-phosphate dehydrogenase of EAC cells by NAD or glutaraldehyde were unsuccessful.
 ...
PMID:Purification and characterization of 3-phosphoglycerate kinase from Ehrlich ascites carcinoma cells. 2290 79