Vlm. Lima et al., IMMOBILIZED CRATYLIA-MOLLIS LECTIN AS A POTENTIAL MATRIX TO ISOLATE PLASMA GLYCOPROTEINS, INCLUDING LECITHIN-CHOLESTEROL ACYLTRANSFERASE, Carbohydrate polymers, 33(1), 1997, pp. 27-32
A crude seed extract from the native Brazilian forage, Cratylia mollis
Mart., and its purified lectin (termed Cra), were found to precipitat
e glycoproteins from serum. An affinity column of Cra lectin coupled t
o Sepharose CL-4B was prepared and its ability to isolate glycoprotein
s from human plasma compared to that of a commercial immobilized lecti
n, Concanavalin (Con) A-Sepharose. Although both lectins are of the al
pha-D-mannose/alpha-D-glucose binding class, clear differences in the
type and amount of serum glycoproteins adsorbed were seen on analysis
by denaturing polyacrylamide gel electrophoresis. Similarly, when a se
mipurified preparation of the plasma glycoprotein, lecithin-cholestero
l acyltransferase (LCAT, EC 2.3.1.43) was applied to the columns some
differences were evident; most LCAT was not retained by either matrix
but when the bound fractions were eluted and analyzed electrophoretica
lly the LCAT isolated by the Cra-Sepharose column was much purer. Thes
e findings suggest that immobilized Cra lectin has the potential for u
se in studies both to isolate and to characterize certain serum glycop
roteins. (C) 1997 Elsevier Science Ltd.