Agrius convolvuli haemolymph ferritin was purified by KBr density gradient ultracentrifugation and anion exchange column chromatography. The 670kDa ferritin was composed of two subunits of 26kDa and 31kDa. It was also shown that the protein had an isoelectric point (pI) of pH 7.4. The N-terminal amino acid sequences of the two subunits were NH$_2$- DNXYQDVSLDXSQAXNXL and (26kDa subunit) and NH$_2$-TQXHVNPVNIQRDXVTMHXS (31kDa subunit). The sequential analysis showed that they had high similarity to lepidopteran ferritin subunits, S- and G-type, respectively. Using electron microscope, it was observed that the protein had a core whose size was about 7nm. In the amino acid composition of the protein, Glu (13.22%), Asp (10.43%), Pro (9.69%), Leu (9.63%), Ala (9.55%) and Gly (8.49%) were in relatively highv contents while Tyr(l.21%), His (2.58%) and Arg (3.10%) were in low. It was shown that the amount of ferritin in A. convolvuli haemolymph was increased by injection of eight different heavy metal ions, FeCl$_3$, HgCl$_2$, CuSO$_4$, ZnSO$_4$, MnCl$_2$, MgCl$_2$, CrCl$_3$ and CdCl$_2$. Among the ions, Fe$^$3+/, Hg$^$2+/, Zn$^$4+/, Mn$^$2+/ and Cd$^$2+/ significantly induced the amount of the protein.