Peptide transporter 1 (PEPT1) function is well understood, yet little is known about its contribution toward the absorption of dietary amino acids in the form of di- and tripeptides. In the present human study, changes in plasma concentrations of a
Journal of neurochemistry, 56(1), 129-135 (1991-01-01)
Canavan disease, an autosomal recessive disorder, is characterized biochemically by N-acetylaspartic aciduria and aspartoacylase (N-acyl-L-aspartate amidohydrolase; EC 3.5.1.15) deficiency. However, the role of aspartoacylase and N-acetylaspartic acid in brain metabolism is unknown. Aspartoacylase has been purified to apparent homogeneity with
The title bis(glycyl-L-aspartic acid) oxalate complex {systematic name: bis[2-(2-ammonioacetamido)butanedioic acid] oxalate 0.4-hydrate}, 2C6H11N2O5+.C2O4(2-).4H2O, crystallizes in a triclinic space group with the planar peptide unit in a trans conformation. The asymmetric unit consists of two glycyl-L-aspartic acid molecules with positively charged
Journal of inorganic biochemistry, 77(3-4), 135-139 (2000-03-04)
The first solution studies at physiological pH for the formation of metal complexes of taurine, +NH3CH2CH2S03-, one of the most abundant low molecular weight organic compounds in the animal kingdom, are reported. The complexes Cu(Gly-GlyH-1) (1) and [Cu(Gly-AspH-1)] (2) react
International journal of peptide and protein research, 19(2), 206-211 (1982-02-01)
The crystal structure of the acidic dipeptide glycyl-L-aspartic acid dihydrate, Gly-L-Asp X 2H2O, C6H10N2O5 X 2H2O, has been determined by means of three-dimensional counter X-ray data. The dipeptide crystallizes in space group P212121 of the orthorhombic system with four formula
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