MCD-PEPTIDE FROM BEE VENOM - ISOLATION BIOCHEMICAL AND PHARMACOLOGICAL PROPERTIES

Bee venom contains three agents which can produce mast cell degranulation. Melittin is a universally acting surfactant; phospholipase A releases the mastocytolytic lysolecithin. A third mast cell degranulating (MCD) peptide has been isolated by gel filtration on Sephadex G 50, followed by chromatography on carboxymethylcellulose, and, finally, on Amberlite IRC-50. MCD-peptide is strongly basic (isoelectric point near pH 12). From the amino acid analysis, a minimum molecular weight of 2593 has been calculated. MCD-peptide consists of 22 amino acids, among them 4 halfcystine residues. It can be obtained in two fractions differing by charge, which appear homogeneous, however, on paper chromatography, paper electrophoresis, and amino acid analysis. When tested on isolated mast cells or on mesentery tissue of rats, MCD-peptide is equiactive with compound 48/80. On the other hand, melittin is 100 times less potent than compound 48/80 on the former tissue and 10 times less potent on the latter; moreover, the dose-response-relation of histamine release is flatter with melittin. MCD-peptide and compound 48/80 depress the blood pressure of rats in a quantitatively and qualitatively similar manner. Crossed tachyphylaxis has been demonstrated. Both substances increase the capillary permeability of rat skin upon intracutaneous injection. Melittin is less active on rat skin vessels. The skin capillaries of rabbits are, however, more sensitive to melittin and compound 48/80 than to MCD-peptide. MCD-peptide (0.5-10 mg/kg i.v.) produces in rats an extreme cyanosis of the acra. A short lasting spasm of the extremities points to an additional effect on the motor system of rats. © 1968 Springer-Verlag.