p0720  (New England Biolabs)

Journal: ACS Infectious Diseases

Article Title: Elucidation of a Human Urine Metabolite as a Seryl-Leucine Glycopeptide and as a Biomarker of Effective Anti-Tuberculosis Therapy

doi: 10.1021/acsinfecdis.8b00241

Figure Lengend Snippet: Confirmation of seryl-leucine peptide and SLC1G structure. EIC for m / z 219.1328 in LC-MS spectra of α2-3,6,8 neuraminidase and O -glycosidase treated MF 874.3547 (A) and seryl-leucine standard (C). MS/MS of m / z 219.1328 from α2-3,6,8 neuraminidase and O -glycosidase treated MF 874.3547 (B) and the seryl-leucine standard (D). The confirmed structure of Neu5Acα2-3Galβ1-3GalNAcα1- O -SerLeu for MF 874.3547 (E).

Article Snippet: MF 874.3547 (9 μL) or standards (60 ng) of 4-nitrophenyl O -(N -acetyl-α-neuraminosyl)-(2-6)-β-d -galactopyranosyl-(1-4)-2-acetamido-2-deoxy-β-d -glucopyranoside (EN4614, Carbosynth Ltd., San Diego, CA), glycan-F58 (ULM-10078-CA, Cambridge Isotope Laboratories, Inc., Tewksbury, MA), and Sialo Anti-Proliferative Factor (GP131025, Sussex Research Laboratories, Ottawa, ON) were treated with α2-3 neuraminidase S (PO743S), α2-3,6,8 neuraminidase (#P0720S, New England Biolabs Inc., Ipswich, MA, USA), and O -glycosidase (#P0733S, New England Biolabs Inc.).

Techniques: Liquid Chromatography with Mass Spectroscopy, Mass Spectrometry

Journal: ACS Infectious Diseases

Article Title: Elucidation of a Human Urine Metabolite as a Seryl-Leucine Glycopeptide and as a Biomarker of Effective Anti-Tuberculosis Therapy

doi: 10.1021/acsinfecdis.8b00241

Figure Lengend Snippet: Enzymatic deglycosylation and MS confirmation of core 1 glycosylation. MF 874.3547 untreated (A, C, E, G, I) and treated with α2-3,6,8 neuraminidase and O -glycosidase (B, D, F, H, J) were analyzed by LC-MS, and the spectra were evaluated by extracted ion chromatogram (EIC) for intact glycopeptide (A and B), the glycopeptide minus Neu5Ac (C and D), the Hex–HexNAc disaccharide (E and F), Neu5Ac (G and H), and the deglycosylated putative diamino acid S/TX (I and J). The * in panel C indicates a low level of the glycopeptide minus Neu5Ac ( m / z 584.2661) present in the undigested sample. Note the level of this product was considerably higher following digestion (G). In source fragmentation of SLC1G yielded the m / z 584.2661 product (# in panel C) at the same retention time as the undigested glycopeptide.

Article Snippet: MF 874.3547 (9 μL) or standards (60 ng) of 4-nitrophenyl O -(N -acetyl-α-neuraminosyl)-(2-6)-β-d -galactopyranosyl-(1-4)-2-acetamido-2-deoxy-β-d -glucopyranoside (EN4614, Carbosynth Ltd., San Diego, CA), glycan-F58 (ULM-10078-CA, Cambridge Isotope Laboratories, Inc., Tewksbury, MA), and Sialo Anti-Proliferative Factor (GP131025, Sussex Research Laboratories, Ottawa, ON) were treated with α2-3 neuraminidase S (PO743S), α2-3,6,8 neuraminidase (#P0720S, New England Biolabs Inc., Ipswich, MA, USA), and O -glycosidase (#P0733S, New England Biolabs Inc.).

Techniques: Mass Spectrometry, Liquid Chromatography with Mass Spectroscopy

Journal: Carbohydrate research

Article Title: Improved isolation and characterization procedure of sialylglycopeptide from egg yolk powder

doi: 10.1016/j.carres.2017.10.001

Figure Lengend Snippet: Determining the position of the hexose on the isolated SGP. A The isolated SGP could be treated with pronase (top) to trim the peptide down to Asn or PNGase F (bottom) to remove the peptide completely. B The LC-MS chromatogram of pronase treated SGP, showing disappearance of the additional hexose. C ESI of the cleaved peptide from isolated SGP with PNGase F. The peak at 821 corresponds to the peptide with hexose.

Article Snippet: Neuraminidase ( Clostridium perfringens ), #P0720 and PNGase F ( Flavobacterium meningosepticum) , #P0704 were from New England Biolabs.

Techniques: Isolation, Liquid Chromatography with Mass Spectroscopy