The N-glycosylation of mouse immunoglobulin G (IgG)-fragment crystallizable differs between IgG subclasses and Strains

Frontiers in Immunology

Volumn 8, Issue MAY, 2017, Pages

  de Haan, Noortje ^a   Reiding, Karli R ^a   Krištić, Jasminka ^b   Ederveen, Agnes L Hipgrave ^a   Lauc, Gordan ^b   Wuhrer, Manfred ^a  

^a LEIDEN UNIVERSITY MEDICAL CENTER   (Netherlands)

^b GENOS GLYCOSCIENCE RESEARCH LABORATORY   (Croatia)

Author keywords

Fc glycosylation; Glycopeptides; HILIC UPLC fluorescence; Immunoglobulin G; LC MS; MALDI TOF MS; Mouse; N glycans

Indexed keywords

IMMUNOGLOBULIN FC FRAGMENT; IMMUNOGLOBULIN G; IMMUNOGLOBULIN G1; IMMUNOGLOBULIN G2A; IMMUNOGLOBULIN G2B; IMMUNOGLOBULIN G3;

ARTICLE; FEMALE; GENDER; HYDROPHILIC INTERACTION CHROMATOGRAPHY; INFORMATION PROCESSING; LIQUID CHROMATOGRAPHY-MASS SPECTROMETRY; MALE; MATRIX ASSISTED LASER DESORPTION IONIZATION TIME OF FLIGHT MASS SPECTROMETRY; MOUSE; NANOLIQUID CHROMATOGRAPHY MASS SPECTROMETRY; NONHUMAN; POLYACRYLAMIDE GEL ELECTROPHORESIS; PROTEIN GLYCOSYLATION; SIALYLATION; SOLID PHASE EXTRACTION; ULTRA PERFORMANCE LIQUID CHROMATOGRAPHY;

EID: 85019981733     PISSN: None     EISSN: 16643224     Source Type: Journal    
DOI: 10.3389/fimmu.2017.00608     Document Type: Article

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