Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Pivot Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Target Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Query: EC:3.2.1.23 (
beta-galactosidase
)
14,648
document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)
4-(N-Methylcoumarin-7-yl) glycamines were employed in studying asparagine-linked carbohydrate chains of acid desialylated fetuin. The procedure was optimised for the reductive amination of oligosaccharides with 7-amino-4-methylcoumarin in the presence of Na(CN)BH3 to lead to oligosaccharide glycamines (
AMC
-OS).
AMC
-OS were obtained from dextran oligosaccharides and from oligosaccharides released by hydrazinolysis of asparagine-linked sugar chains of asialofetuin. Reverse-phase HPLC and exclusion HPLC with fluorimetric quantitation of
AMC
-OS is described. TSK Gel 2000 SW column was calibrated using dextran
AMC
-OS to give linear relationship ln Ni = k(ti/tr)+b, where ti/tr is retention time of the
AMC
-OS relatively to the reference
AMC
-trisaccharide, and Ni is calibration unit value, characterizing molecular size of
AMC
-OS. Three
AMC
-OS, Gal3GlcNAc3Man3GlcNAc2-
AMC
(I) and (II), and Gal2GlcNAc3Man3GlcNAc2AMC (III), were obtained from asialofetuin in a molar ration of 1:1.8:0.1. Acid treatment of AMK-OS (II) in desialylation conditions also gave
AMC
-OS (III), thus suggesting a partial degalactosylation of the glycoprotein sugar chains during the desialylation. Consequent digestion of
AMC
-OS (II) and (III) with Jack bean
beta-galactosidase
and beta-N-acetylhexosaminidase led to the same
AMC
-OS, Man3GlcNAc2AMC. The final digestion product of
AMC
-OS (I) was GalGlcNAcMan3GlcNAc2AMC, suggesting a structural difference in one of the antennas of the minor sugar chain of asialofetuin. The monosaccharide quantitation and exoglycosidase sequencing were carried out at a 100 pmole level.
...
PMID:[Fluorescent derivatives of carbohydrates in the analysis of the structure of glycoconjugates. N-(4-methylcoumarin-7-yl) glycamines in the study of asparagine-bound carbohydrate chains of glycoproteins]. 342 43