The non-degradative isolation of α1-acid glycoprotein from normal and rheumatoid plasma

M A  ELLIOTT; H G  ELLIOTT; C M  MCLAUGHLIN; Y M  STEWART; K D  SMITH

doi:10.1080/07328309508005365

The non-degradative isolation of α1-acid glycoprotein from normal and rheumatoid plasma

M A ELLIOTT, H G ELLIOTT, C M MCLAUGHLIN, Y M STEWART, K D SMITH

Strathclyde Institute Of Pharmacy And Biomedical Sciences

Research output: Contribution to journal › Article › peer-review

6 Citations (Scopus)

Abstract

We have developed a method for the purification of alpha(1)-acid glycoprotein (AGP) using procedures unlikely to damage the glycoprotein structure. This was utilised to isolate AGP from samples of normal and rheumatoid plasma. The effectiveness of the purification procedure was examined by enzymatically deglycosylating each sample of AGP, separating the released oligosaccharides by chromatography on a pellicular high pH anion-exchange (HPAE) resin at pH 13 and detecting by a pulsed electrochemical (PED) method. The analytical profile for normal AGP was consistent with those previously reported thus indicating that the purification procedure did not denature the oligosaccharide chains of AGP; there was a noticeable difference between AGP in normal and rheumatoid plasma.

Original language	English
Pages (from-to)	643-652
Number of pages	10
Journal	Journal of Carbohydrate Chemistry
Volume	14
Issue number	4-5
DOIs	https://doi.org/10.1080/07328309508005365
Publication status	Published - 1995

Keywords

glycoproteins
inflammation
disease
rheumatoid plasma

Access to Document

10.1080/07328309508005365

Cite this

@article{b4eeadab2a6a4d29a49465e226ec18d5,

title = "The non-degradative isolation of α1-acid glycoprotein from normal and rheumatoid plasma",

abstract = "We have developed a method for the purification of alpha(1)-acid glycoprotein (AGP) using procedures unlikely to damage the glycoprotein structure. This was utilised to isolate AGP from samples of normal and rheumatoid plasma. The effectiveness of the purification procedure was examined by enzymatically deglycosylating each sample of AGP, separating the released oligosaccharides by chromatography on a pellicular high pH anion-exchange (HPAE) resin at pH 13 and detecting by a pulsed electrochemical (PED) method. The analytical profile for normal AGP was consistent with those previously reported thus indicating that the purification procedure did not denature the oligosaccharide chains of AGP; there was a noticeable difference between AGP in normal and rheumatoid plasma.",

keywords = "glycoproteins, inflammation, disease, rheumatoid plasma",

author = "ELLIOTT, {M A} and ELLIOTT, {H G} and MCLAUGHLIN, {C M} and STEWART, {Y M} and SMITH, {K D}",

year = "1995",

doi = "10.1080/07328309508005365",

language = "English",

volume = "14",

pages = "643--652",

journal = "Journal of Carbohydrate Chemistry ",

issn = "0732-8303",

publisher = "Taylor and Francis Ltd.",

number = "4-5",

}

TY - JOUR

T1 - The non-degradative isolation of α1-acid glycoprotein from normal and rheumatoid plasma

AU - ELLIOTT, M A

AU - ELLIOTT, H G

AU - MCLAUGHLIN, C M

AU - STEWART, Y M

AU - SMITH, K D

PY - 1995

Y1 - 1995

N2 - We have developed a method for the purification of alpha(1)-acid glycoprotein (AGP) using procedures unlikely to damage the glycoprotein structure. This was utilised to isolate AGP from samples of normal and rheumatoid plasma. The effectiveness of the purification procedure was examined by enzymatically deglycosylating each sample of AGP, separating the released oligosaccharides by chromatography on a pellicular high pH anion-exchange (HPAE) resin at pH 13 and detecting by a pulsed electrochemical (PED) method. The analytical profile for normal AGP was consistent with those previously reported thus indicating that the purification procedure did not denature the oligosaccharide chains of AGP; there was a noticeable difference between AGP in normal and rheumatoid plasma.

AB - We have developed a method for the purification of alpha(1)-acid glycoprotein (AGP) using procedures unlikely to damage the glycoprotein structure. This was utilised to isolate AGP from samples of normal and rheumatoid plasma. The effectiveness of the purification procedure was examined by enzymatically deglycosylating each sample of AGP, separating the released oligosaccharides by chromatography on a pellicular high pH anion-exchange (HPAE) resin at pH 13 and detecting by a pulsed electrochemical (PED) method. The analytical profile for normal AGP was consistent with those previously reported thus indicating that the purification procedure did not denature the oligosaccharide chains of AGP; there was a noticeable difference between AGP in normal and rheumatoid plasma.

KW - glycoproteins

KW - inflammation

KW - disease

KW - rheumatoid plasma

U2 - 10.1080/07328309508005365

DO - 10.1080/07328309508005365

M3 - Article

SN - 0732-8303

VL - 14

SP - 643

EP - 652

JO - Journal of Carbohydrate Chemistry

JF - Journal of Carbohydrate Chemistry

IS - 4-5

ER -

The non-degradative isolation of α1-acid glycoprotein from normal and rheumatoid plasma

Abstract

Keywords

Access to Document

Fingerprint

Cite this