“…Molecular nature of all the six naturally occurring lectins isolated from human plasma/serum have been studied by estimating the native molecular weight using various methods including analytical ultracentrifugation, gel filtration, sucrose gradient centrifugation and polyacrylamide gradient gel electrophoresis. Accordingly, the native molecular weight estimates for various lectins are: 118–140 kDa for C-reactive protein ( Gotschlich and Edelman, 1965 ; Siegel et al., 1974 ), 240–300 kDa for serum amyloid protein ( Hamazaki, 1986 ; Binette et al., 1974 ), 520–688 kDa for H-ficolin ( Yae et al., 1991 ), 200–700 kDa for mannan-binding lectin ( Taylor and Summerfield, 1987 ; Thiel et al., 1992 ), 68 or 90 kDa for tetranectin ( Clemmensen et al., 1986 ; Thougaard et al., 2001 ) and 320 or 650 kDa for L-ficolin ( Matsushita et al., 1996 ; Krarup et al., 2004 ). The analysis of subunit characteristics mostly by SDS-PAGE under reducing conditions revealed that various isolated lectin molecules are composed of identical subunits, but the number of subunits in different lectins varied between 3 and 22 ( Thougaard et al., 2001 ; Super et al., 1989 ) and each subunit with molecular mass ranging from 20 to 40 kDa ( Gotschlich and Edelman, 1965 ; Le et al., 1997 ).…”