Purification of a Lectin from the Hemolymph of Chinese Oak Silk Moth (Antheraea pernyi) Pupae
- 1 March 1987
- journal article
- research article
- Published by Oxford University Press (OUP) in The Journal of Biochemistry
- Vol. 101 (3) , 545-551
- https://doi.org/10.1093/jb/101.3.545
Abstract
A lectin with affinity to galactose was purified to homogeneity from the hemolymph of diapausing pupae of the Chinese oak silk moth, Antheraea pernyi. The molecular mass of this lectin was 380,000 and it formed an oligomeric structure of a subunit with a molecular mass of 38,000. The hemagglutinating activity in the hemolymph was found to increase with time after immunization with E. coli. Studies with antibody against the purified lectin showed that increase in the hemagglutinating activity was due to the same lectin, suggesting that the amount of the lectin increased in response to intrusion of foreign substances. The function of this lectin in the defence mechanism is discussed.Keywords
This publication has 6 references indexed in Scilit:
- A new multimeric hemagglutinin from the coelomic fluid of the sea urchin Anthocidaris crassispinaBiochemistry, 1985
- Purification and Characterization of a Lectin from the Beetle, Allomyrina dichotomaThe Journal of Biochemistry, 1984
- Identification of a Protein Having Hemagglutinating Activity in the Hemolymph of the Silkworm, Bombyx mori1The Journal of Biochemistry, 1983
- Measurement of Sarcophaga peregrina lectin under various physiological conditions by radioimmunoassay.Journal of Biological Chemistry, 1983
- The specificity of the serum agglutinins of Periplaneta americana and Schistocerca gregaria and its relationship to the insects' immune responseJournal of Insect Physiology, 1981
- Isolation and characterization of a hemagglutinin from Limulus polyphemusJournal of Molecular Biology, 1968