PMID- 28785176
OWN - NLM
STAT- MEDLINE
DCOM- 20180502
LR  - 20181113
IS  - 1943-4731 (Electronic)
IS  - 1524-0215 (Print)
IS  - 1524-0215 (Linking)
VI  - 28
IP  - 3
DP  - 2017 Sep
TI  - Predicting the Retention Behavior of Specific O-Linked Glycopeptides.
PG  - 122-126
LID - 10.7171/jbt.17-2803-003 [doi]
AB  - O-Linked glycosylation is a common post-translational modification that can alter 
      the overall structure, polarity, and function of proteins. Reverse-phase (RP) 
      chromatography is the most common chromatographic approach to analyze 
      O-glycosylated peptides and their unmodified counterparts, even though this 
      approach often does not provide adequate separation of these two species. 
      Hydrophilic interaction liquid chromatography (HILIC) can be a solution to this 
      problem, as the polar glycan interacts with the polar stationary phase and 
      potentially offers the ability to resolve the peptide from its modified form(s). 
      In this paper, HILIC is used to separate peptides with O-N-acetylgalactosamine 
      (O-GalNAc), O-N-acetylglucosamine (O-GlcNAc), and O-fucose additions from their 
      native forms, and coefficients representing the extent of hydrophilicity were 
      derived using linear regression analysis as a means to predict the retention 
      times of peptides with these modifications.
FAU - Badgett, Majors J
AU  - Badgett MJ
AD  - Complex Carbohydrate Research Center, University of Georgia, Athens, Georgia 
      30602, USA; and.
FAU - Boyes, Barry
AU  - Boyes B
AD  - Complex Carbohydrate Research Center, University of Georgia, Athens, Georgia 
      30602, USA; and.
AD  - Advanced Materials Technology, Wilmington, Delaware 19810, USA.
FAU - Orlando, Ron
AU  - Orlando R
AD  - Complex Carbohydrate Research Center, University of Georgia, Athens, Georgia 
      30602, USA; and.
LA  - eng
GR  - R41 GM119879/GM/NIGMS NIH HHS/United States
GR  - R44 GM093747/GM/NIGMS NIH HHS/United States
PT  - Journal Article
DEP - 20170804
PL  - United States
TA  - J Biomol Tech
JT  - Journal of biomolecular techniques : JBT
JID - 100888641
RN  - 0 (Glycopeptides)
RN  - 0 (Polysaccharides)
RN  - 28RYY2IV3F (Fucose)
RN  - KM15WK8O5T (Acetylgalactosamine)
RN  - V956696549 (Acetylglucosamine)
SB  - IM
MH  - Acetylgalactosamine/*chemistry
MH  - Acetylglucosamine/*chemistry
MH  - Amino Acid Sequence/genetics
MH  - Chromatography, Liquid
MH  - Chromatography, Reverse-Phase
MH  - Fucose/chemistry
MH  - Glycopeptides/*chemistry/genetics/isolation & purification
MH  - Glycosylation
MH  - Hydrophobic and Hydrophilic Interactions
MH  - Polysaccharides/chemistry/genetics
MH  - Protein Processing, Post-Translational/genetics
PMC - PMC5544176
OTO - NOTNLM
OT  - HILIC
OT  - Hydrophilic Interaction Chromatography
OT  - LC-MS
EDAT- 2017/08/09 06:00
MHDA- 2018/05/03 06:00
PMCR- 2017/09/01
CRDT- 2017/08/09 06:00
PHST- 2017/08/09 06:00 [pubmed]
PHST- 2018/05/03 06:00 [medline]
PHST- 2017/08/09 06:00 [entrez]
PHST- 2017/09/01 00:00 [pmc-release]
AID - JBT_2017-2803-003 [pii]
AID - 10.7171/jbt.17-2803-003 [doi]
PST - ppublish
SO  - J Biomol Tech. 2017 Sep;28(3):122-126. doi: 10.7171/jbt.17-2803-003. Epub 2017 
      Aug 4.