Results 101 to 110 of about 17,182 (211)

Using atomistic solution scattering modelling to elucidate the role of the Fc glycans in human IgG4.

open access: yesPLoS ONE
Human immunoglobulin G (IgG) exists as four subclasses IgG1-4, each of which has two Fab subunits joined by two hinges to a Fc subunit. IgG4 has the shortest hinge with 12 residues.
Valentina A Spiteri   +6 more
doaj   +1 more source

Fragments of bacterial endoglycosidase S and immunoglobulin G reveal subdomains of each that contribute to deglycosylation [PDF]

open access: yes, 2014
Endoglycosidase S (EndoS) is a glycoside-hydrolase secreted by the bacterium Streptococcus pyogenes. EndoS preferentially hydrolyzes the N-linked glycans from the Fc region of IgG during infection. This hydrolysis impedes Fc functionality and contributes
Yu, Xiaojie   +13 more
core   +1 more source

A newly isolated human intestinal bacterium strain capable of deglycosylating flavone C-glycosides and its functional properties

open access: yesMicrobial Cell Factories, 2019
Background Flavone C-glycosides are difficult to be deglycosylated using traditional chemical methods due to their solid carbon–carbon bond between sugar moieties and aglycones; however, some bacteria may easily cleave this bond because they generate ...
Shiqi Zheng   +5 more
doaj   +1 more source

Effects of deglycosylation of human thyroperoxidase on its enzymatic activity and immunoreactivity.

open access: yes, 1992
International audienceThyroid peroxidase (TPO) is a glycoprotein enzyme which catalyses the iodination of thyroglobulin and the coupling of iodinated tyrosines.
Long, Y   +3 more
core  

Partial deglycosylation of blood-group-specific glycoproteins [PDF]

open access: yesBiochemical Journal, 1980
The time course for the partial deglycosylation of blood-group-specific glycoproteins from human ovarian-cyst fluids with 0.25 M-H2SO4/acetic acid and 6 M-HCl in methanol was studied. Either reagent readily removed about 80% of the carbohydrate from the glycoproteins to leave non-diffusible glycopeptides that contain N-acetylgalactosamine as the ...
openaire   +2 more sources

Expression and purification of PNGase F( PNGase F) in escherichia coli and its functional study

open access: yes上海师范大学学报. 自然科学版, 2013
N-glycosidase F(PNGase F)is a enzyme of deglycosylation,secreted by the gram-negative bacterium Flavobacterium meningosepticum.It’s theoretical molecular weight is about 34.8 kDa.In this study,the PNGase F gene of 945 bp was amplified by PCR technique.A ...
MIN Weiyong, LIU Li, ZHANG Zhou
doaj  

Deglycosylation of ovalbumin prohibits formation of a heat-stable conformer

open access: yes, 2007
To study the influence of the carbohydrate-moiety of ovalbumin on the formation of the heat-stable conformer S-ovalbumin, ovalbumin is deglycosylated with PNGase-F under native conditions.
de Groot, J.   +4 more
core   +2 more sources

N-Glycosylation Site Analysis of Proteins from Saccharomyces cerevisiae by Using Hydrophilic Interaction Liquid Chromatography-Based Enrichment, Parallel Deglycosylation, and Mass Spectrometry

open access: yes, 2014
N-Glycosylation site analysis of baker's yeast Saccharomyces cerevisiae is of fundamental significance to elucidate the molecular mechanism of human congenital disorders of glycosylation (CDG).
于龙   +7 more
core   +1 more source

Centrifugation Assisted Microreactor Enables Facile Integration of Trypsin Digestion, Hydrophilic Interaction Chromatography Enrichment, and On-Column Deglycosylation for Rapid and Sensitive N-Glycoproteome Analysis

open access: yes, 2012
Sample handling procedures including protein digestion, glycopeptide enrichment, and deglycosylation have significant impact on the performance of glycoproteome analysis.
Wang, Fangjun   +10 more
core   +1 more source

Enzymatic deglycosylation of soy proteins as a method to increase the efficiency of their hydrolysis

open access: yesТонкие химические технологии
Objectives. Soy protein hydrolysates are now widely used in the food industry, fish farming, poultry farming, livestock farming, as well as in medical preparations. The most effective method for their production is enzymatic hydrolysis.
V. N. Leontiev, O. I. Lazovskaya
doaj   +1 more source

Home - About - Disclaimer - Privacy