ABSTRACT
The variety of proteins and peptides isolated from honey bee venom and wasp venom includes melittin, adiapin, apamine, bradykinin, cardiopep, mast cell degranulating peptide, mastoparan, phospholipase A2 and secapin. Some of the activities they demonstrate may find therapeutic applications.
Subject(s)
Bee Venoms/pharmacology , Bees/metabolism , Peptides/pharmacology , Wasp Venoms/pharmacology , Wasps/metabolism , Animals , Anti-Infective Agents/chemistry , Anti-Infective Agents/pharmacology , Anti-Inflammatory Agents/chemistry , Anti-Inflammatory Agents/pharmacology , Antineoplastic Agents/chemistry , Antineoplastic Agents/pharmacology , Bee Venoms/chemistry , Humans , Neuroprotective Agents/chemistry , Neuroprotective Agents/pharmacology , Wasp Venoms/chemistryABSTRACT
An agglutinin with a molecular mass of 130 kDa has been isolated from the seeds of Alpinia zerumbet cv.'Variegata'. The isolation procedure involved anion exchange chromatography on DEAE-cellulose, affinity chromatography on Affi-gel blue gel, and gel filtration by fast protein liquid chromatography on Superdex 75. The agglutinin exhibited hemagglutinating activity toward rabbit erythrocytes which could not be inhibited by simple sugars. It was composed of four identical 32-kDa subunits with substantial N-terminal sequence similarity to chitinase and yieldin. The hemagglutinating activity of A. zerumbet agglutinin was stable up to 80(o)C and not affected by presence of a variety of salts. The agglutinin stimulated [methyl-(3)H]-thymidine uptake by mouse splenocytes. It did not exhibit antifungal activity.