Proteomic analysis of deglycosylated Proteins in normal human serum using anhydrous hydrogen fluoride treatment

Deglycosylation with anhydrous hydrogen fluoride (HF) is an alternative method for removing oligosaccharides from glycoproteins which can be extremely useful for identification of proteins and the biological roles of post-translational modifications. In this study, a glycosylated proteome of human s...

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Main Authors: Sriyam Supawadee, Supachok Sinchaikul, Payungsak Tantipaiboonwong, Suree Phutrakul, Shui Tein Chen
Format: Journal
Published: 2018
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http://cmuir.cmu.ac.th/jspui/handle/6653943832/60175
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spelling th-cmuir.6653943832-601752018-09-10T03:48:39Z Proteomic analysis of deglycosylated Proteins in normal human serum using anhydrous hydrogen fluoride treatment Sriyam Supawadee Supachok Sinchaikul Payungsak Tantipaiboonwong Suree Phutrakul Shui Tein Chen Biochemistry, Genetics and Molecular Biology Chemistry Materials Science Mathematics Physics and Astronomy Deglycosylation with anhydrous hydrogen fluoride (HF) is an alternative method for removing oligosaccharides from glycoproteins which can be extremely useful for identification of proteins and the biological roles of post-translational modifications. In this study, a glycosylated proteome of human serum was treated by anhydrous HF to deglycosylate the number of oligosaccharides from glycoproteins which facilitated protein identification using proteomic analysis. In the preliminary result, the high performance liquid chromatography (HPLC) and liquid chromatography mass spectrometry (LC-MS) showed that there was no cleavage of disulfide bonds in HF-treated insulin as a negative control. The effect of HF deglycosylation on electrophoresis pattern was studied by resolving on one-dimensional (1-D) and two-dimensional (2-D) gels. Deglycosylation of glycoproteins in human serum resulted in different protein patterns on 1-DE and 2-DE gels with the clearer protein patterns and low amount of complexity. The deglycosylated serum proteins could be enriched and identified by MS analysis. Using this approach, it indicated that the proteins in human serum have some glycosylation that affected to the protein analysis and might possess the diverse biological functions. Therefore, this deglycosylation technique is an effective method to solve the problem of oligosaccharide interference in proteome analysis and be able to use for further glycan analysis. 2018-09-10T03:39:00Z 2018-09-10T03:39:00Z 2008-05-01 Journal 01252526 2-s2.0-67650333136 https://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=67650333136&origin=inward http://cmuir.cmu.ac.th/jspui/handle/6653943832/60175
institution Chiang Mai University
building Chiang Mai University Library
country Thailand
collection CMU Intellectual Repository
topic Biochemistry, Genetics and Molecular Biology
Chemistry
Materials Science
Mathematics
Physics and Astronomy
spellingShingle Biochemistry, Genetics and Molecular Biology
Chemistry
Materials Science
Mathematics
Physics and Astronomy
Sriyam Supawadee
Supachok Sinchaikul
Payungsak Tantipaiboonwong
Suree Phutrakul
Shui Tein Chen
Proteomic analysis of deglycosylated Proteins in normal human serum using anhydrous hydrogen fluoride treatment
description Deglycosylation with anhydrous hydrogen fluoride (HF) is an alternative method for removing oligosaccharides from glycoproteins which can be extremely useful for identification of proteins and the biological roles of post-translational modifications. In this study, a glycosylated proteome of human serum was treated by anhydrous HF to deglycosylate the number of oligosaccharides from glycoproteins which facilitated protein identification using proteomic analysis. In the preliminary result, the high performance liquid chromatography (HPLC) and liquid chromatography mass spectrometry (LC-MS) showed that there was no cleavage of disulfide bonds in HF-treated insulin as a negative control. The effect of HF deglycosylation on electrophoresis pattern was studied by resolving on one-dimensional (1-D) and two-dimensional (2-D) gels. Deglycosylation of glycoproteins in human serum resulted in different protein patterns on 1-DE and 2-DE gels with the clearer protein patterns and low amount of complexity. The deglycosylated serum proteins could be enriched and identified by MS analysis. Using this approach, it indicated that the proteins in human serum have some glycosylation that affected to the protein analysis and might possess the diverse biological functions. Therefore, this deglycosylation technique is an effective method to solve the problem of oligosaccharide interference in proteome analysis and be able to use for further glycan analysis.
format Journal
author Sriyam Supawadee
Supachok Sinchaikul
Payungsak Tantipaiboonwong
Suree Phutrakul
Shui Tein Chen
author_facet Sriyam Supawadee
Supachok Sinchaikul
Payungsak Tantipaiboonwong
Suree Phutrakul
Shui Tein Chen
author_sort Sriyam Supawadee
title Proteomic analysis of deglycosylated Proteins in normal human serum using anhydrous hydrogen fluoride treatment
title_short Proteomic analysis of deglycosylated Proteins in normal human serum using anhydrous hydrogen fluoride treatment
title_full Proteomic analysis of deglycosylated Proteins in normal human serum using anhydrous hydrogen fluoride treatment
title_fullStr Proteomic analysis of deglycosylated Proteins in normal human serum using anhydrous hydrogen fluoride treatment
title_full_unstemmed Proteomic analysis of deglycosylated Proteins in normal human serum using anhydrous hydrogen fluoride treatment
title_sort proteomic analysis of deglycosylated proteins in normal human serum using anhydrous hydrogen fluoride treatment
publishDate 2018
url https://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=67650333136&origin=inward
http://cmuir.cmu.ac.th/jspui/handle/6653943832/60175
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