Title : Chemoselective ligation reaction of N-acetylglucosamine (NAG) with hydrazide functional probes to determine galactosyltransferase activity by MALDI mass spectrometry.

Pub. Date : 2017 Jul 10

PMID : 28692093






5 Functional Relationships(s)
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1 Chemoselective ligation reaction of N-acetylglucosamine (NAG) with hydrazide functional probes to determine galactosyltransferase activity by MALDI mass spectrometry. Isoniazid N-acetyl-alpha-glucosaminidase Homo sapiens
2 We report here the use of synthetic beta-N-acetylglucosamine (NAG) ligands that contain hydrazide functional groups to determine galactosyltransferase activity by mass spectrometry. Isoniazid N-acetyl-alpha-glucosaminidase Homo sapiens
3 We report here the use of synthetic beta-N-acetylglucosamine (NAG) ligands that contain hydrazide functional groups to determine galactosyltransferase activity by mass spectrometry. Isoniazid N-acetyl-alpha-glucosaminidase Homo sapiens
4 With hydrazide-linked beta-d-NAG as the acceptor, the activity of beta-1,4-GT is quantified by matrix-assisted laser desorption/ionization (MALDI)-time-of-flight (TOF) mass spectrometry (MS) with high efficiency. Isoniazid N-acetyl-alpha-glucosaminidase Homo sapiens
5 This is the first work that uses hydrazide-linked beta-d-NAG for activity analysis, providing a new surface-based MS approach to determine enzyme activity in a potentially high-throughput manner. Isoniazid N-acetyl-alpha-glucosaminidase Homo sapiens