PURIFICATION AND CHARACTERIZATION OF STORAGE PROTEIN FROM THE HEMOLYMPH OF MAMESTRA-BRASSICAE (LEPIDOPTERA, NOCTUIDAE)

The storage protein of the cabbage moth (M. brassicae L.) was purified from larval haemolymph by anion exchange chromatography, followed by preparative electrophoresis and elution. Histochemical staining reveal ed that the storage protein is a glyco-lipoprotein. SDS-polyacrylamide gel electrophoresis suggested that this protein is composed of two do minant - M(r) 81.9 and 74.6 kD - and five minor - M(r) 64.1, 58.3, 50. 1, 40.8 and 38.2 kD - subunits. Electrofocusing separation showed the presence of these subunits at pH 5.4-6.3. The conformation of the stor age protein was equally stable at pH ranging from 4 to 9. The M. brass icae storage protein is immunologically related to Lymantria dispar ar ylphorin.