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Change of Haemolymph Ferritin of Sweet Potato Hornworm, Agrius convolvuli by Heavy Metals
Author(s) -
CHOI ChiWon,
HAN Jikhyon,
SEO DongHwan,
RYU JaeKwan,
HWANG SeockYeon,
SEO Sook Jae,
YUN ChiYoung
Publication year - 2004
Publication title -
entomological research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.421
H-Index - 20
eISSN - 1748-5967
pISSN - 1738-2297
DOI - 10.1111/j.1748-5967.2004.tb00090.x
Subject(s) - isoelectric point , hemolymph , biology , ferritin , protein subunit , biochemistry , amino acid , isoelectric focusing , molecular mass , metal , chromatography , microbiology and biotechnology , chemistry , gene , enzyme , organic chemistry
Agrius convolvuli haemolymph ferritin was purified by KBr density gradient ultracentrifugation and anion exchange column chromatography. The 670 kDa ferritin was composed of two subunits of 26 kDa and 31 kDa. 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 NH2‐DNXYQDVSLDXSQAXNXL (26 kDa subunit) and NH2‐TQXHVNPVNIQRDXVTMHXS (31 kDa 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 7 nm. 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 high contents while Tyr (1.21%), 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.