Results Glu content at 2,4,8 h were(0.89±0.162),(0.75±0.276),(0.84±0.542)μmol/(g·protein),and there was significant difference compared with corresponding control group(1.30±0.063)μmol/(g·protein)(P< 0.05);
Low-temperature Heat Capacities and Thermochemistry of the Com-plex of Praseodymium Perchlorate with L-α-Glutamic Acid: [Pr_2(Glu)_2(ClO_4)(H_2O)_7](ClO_4)_3·4H_2O
(3)The extracellular accumulation of GLU increased about two-fold afterischemia for 30 min in vitro(from 128±20 to 431 ± 74 nmol·mg ̄(-1) pro min ̄(-1),n=6).
CONVERSION OF ALANINE DEHYDROGENASE TO GLUTAMIC DEHYDROGENASE BY NITROUS ACID INDUCED MUTATION IN BACILLUS SUBTILIS Ⅱ. THE INDUCTIVE FORMATION OF ALANINE DEHYDROGENASE IN GLUTAMIC DEHYDROGENASE-POSITIVE MUTANTS
A library of 363 glycoconjugates and C-nucleosides synthesized by our earlier reported methods were screened for their effect on isolated filarial glutamate cysteine ligase (GCL) and glutathione reductase (GR).
glutamate cysteine ligase (GCL) and γ-glutamyl transpeptidase (γ-GT) from bovine filarial worms Setaria cervi and their counterparts from mammalian liver to known inhibitors i.e.
The glutaminase (EC 3.5.1.2) isolated from seedlings of triticale (Triticalesp.) had a pH optimum of about 8, was inhibited with excess substrate (glutamine), and reaction products (glutamate and NH+4).
The obtained experimental data convincingly confirm that glutamic acid alone, and particularly in a complex with heparin, has a considerable preventive potential and efficiently protects experimental animals with induced diabetes mellitus.
Hydrophobic interaction may be enhanced in the surface region by the hydrophilic amino acid Glu substituted with the hydrophobic amino acid Val, and may be responsible for the improvement of the optimum temperature.
Further analysis shows that there is no association between C825T genotypes and age, body mass index (BMI), Glucose (GLU), Triglyceride (TG), Cholesterol (CHO), systolic blood pressure (SBP) and diastolic blood pressure (DBP).
Their monosaccharide composition (Man : Gal : Glu) was as follows: 10.4 : 0.9 : 1 (polysaccharide from the endosperm) and 4.5 : 0.9 : 1 (polysaccharide from the hulls).
The peptide epitalon (Ala-Glu-Asp-Gly) constructed on the basis of analysis of the epiphysis peptides did not change the intensity of protein synthesis in the cultured hepatocytes.