Lectin affinity chromatography (LAC) offers a tool that aids purification o
f cell surface glycoconjugates in sufficient quantities so that studies add
ressing their structural elucidation could be carried out. It has several a
dvantages over the conventional biochemical methods, such as immunoprecipit
ation and/or immunoaffinity chromatography, used for the purification of va
rious glycoconjugates. Serial LAC (SLAC) not only helps establish the ident
ity of a glycoprotein or allows purification of a glycoprotein to homogenei
ty from among a mixture of glycoproteins, but it also successfully resolves
the microheterogeneity in these glycoproteins, which is an otherwise impra
cticable problem to address. Specific cases of the altered expression and m
aintenance of microheterogeneity of some of the glycoproteins in pathologic
al conditions vis a vis during normal biology are presented. The applicatio
n of LAC in (i) itself, (ii) a serial fashion, and (iii) conjunction with o
ther techniques such as two-dimensional electrophoresis, capillary electrop
horesis, mass spectrometry, etc. in the diagnosis of certain pathological c
onditions, and the possibility of using this knowledge in designing treatme
nts for various diseases, is discussed. (C) 2001 Elsevier Science BN. All r
ights reserved.