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Exploiting lectin affinity chromatography in clinical diagnosis.

Authors
  • Satish, P R1
  • Surolia, A
  • 1 Molecular Biophysics Unit, Indian Institute of Science, Bangalore 560 012, India. , (India)
Type
Published Article
Journal
Journal of Biochemical and Biophysical Methods
Publisher
Elsevier
Publication Date
Oct 30, 2001
Volume
49
Issue
1-3
Pages
625–640
Identifiers
PMID: 11694306
Source
Medline
Language
English
License
Unknown

Abstract

Lectin affinity chromatography (LAC) offers a tool that aids purification of cell surface glycoconjugates in sufficient quantities so that studies addressing their structural elucidation could be carried out. It has several advantages over the conventional biochemical methods, such as immunoprecipitation and/or immunoaffinity chromatography, used for the purification of various glycoconjugates. Serial LAC (SLAC) not only helps establish the identity of a glycoprotein or allows purification of a glycoprotein to homogeneity from among a mixture of glycoproteins, but it also successfully resolves the microheterogeneity in these glycoproteins, which is an otherwise impracticable problem to address. Specific cases of the altered expression and maintenance of microheterogeneity of some of the glycoproteins in pathological conditions vis a vis during normal biology are presented. The application of LAC in (i) itself, (ii) a serial fashion, and (iii) conjunction with other techniques such as two-dimensional electrophoresis, capillary electrophoresis, mass spectrometry, etc. in the diagnosis of certain pathological conditions, and the possibility of using this knowledge in designing treatments for various diseases, is discussed.

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