2002 Volume 68 Issue sup2 Pages 1127-1130
Megabalanus rosa contained the C-type lectins as the major constituents of hemolymph proteins. BRA-1 (330 kDa) and BRA-2 (140 kDa) were composed of identical subunits (173 amino acids), and BRA-3 (64 kDa) of four same subunits (138 amino acids). These lectins were present in various tissues other than the hemolymph. However, only BRA-2 was detected in the organic matrix of shell by western blotting. Both BRA-2 and BRA-3 showed high association constants to calcium ions and inhibitory activity to CaCO3 crystallization. The immobilized BRA-2 was found to promote the CaCO3 crystallization. M. rosa lectins also showed opsonic activity when checked with murine macrophage. The gene structures of BRA-2 and BRA-3 were different from each other. These results suggest the participation in defense as well as biomineralization and the allotted biological role of M. rosa humoral lectins.
