2001 Volume 66 Issue 1 Pages 55-58
Soluble proteins from the specialised reproductive structure, the tuberous roots of Momordica dioica Roxb. through which it propagates, were analysed by SDS-PAGE to compare the protein profiles of the sex forms. Twenty eight bands with molecular masses ranging from 15 kD protein to more than 94 kD proteins were found to be common in both sexes. The difference in their protein profiles was marked by the presence of a 22 kD polypeptide (p-22) in the female sex which was not detected in its male counterpart. Further studies by immunoblot assay demonstrated that antibody raised against p-22 not only cross-reacted at 22 kD antigen of the female sex but also with 29 kD and 32 kD polypeptides of the male and female sex forms. It indicates that these 3 polypeptides are electrophoretically distinct but antigenically similar. 22 kD protein found in female sex is, therefore, not sex specific rather sex linked. Moreover, variation in the intensity of 29 kD and 32 kD polypeptides of male and female sex forms suggests that the interplay of these 2 sex linked polypeptides may be a contributing factor in controlling sex mechanism of dioecious Momordica dioica.