Eur. J. Entomol. 90 (2): 123-135, 1993

Purification and characterization of storage protein from the haemolymph of Mamestra brassicae (Lepidoptera: Noctuidae)

SLOVAK M., REPKA V.
N/A

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 revealed that the storage protein is a glyco-lipoprotein. SDS-polyacrylamide gel electrophoresis suggested that this protein is composed of two dominant - Mr 81.9 and 74.6 kD - and five minor - Mr 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 storage protein was equally stable at pH ranging from 4 to 9. The M. brassicae storage protein is immunologically related to Lymantria dispar arylphorin.

Keywords: Biochemistry, Lepidoptera, Mamestra brassicae, haemolymph, storage proteins, arylphorin

Accepted: February 23, 1993; Published: June 25, 1993  Show citation

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SLOVAK, M., & REPKA, V. (1993). Purification and characterization of storage protein from the haemolymph of Mamestra brassicae (Lepidoptera: Noctuidae). EJE, 90(2), 123-135
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