Abstract
Biliverdin binding protein, cyanoprotein (CP), was purified from egg extracts of the bean bug, Riptortus clavatus. The preparation was shown to be homogeneous by DEAE-chromatography and polyacrylamide gel electrophoresis (PAGE). The native molecular weight (MW) of egg CP (CP egg) was estimated to be 320,000 by PAGE and 335,000 by gel filtration. The apoprotein consisted of identical subunits with MW of 76,000. CP egg had a high content of aromatic amino acids (17% mol ratio) with absorbance peaks at 370 and 620 nm which are characteristic of biliverdins. Native CP egg was associated non-covalently with 16 molecules of biliverdin. CP egg contained about 13.0% neutral sugar (mainly mannose) associated covalently with the apoprotein, no lipid was detected. In the hemolymph of the bugs, four CP bands (CP1, 2, 3 and 4) were detected by native PAGE. These bands were immunologically related and showed properties similar to CP egg in biochemical analysis. Only CP1 was identical to CP egg. CPs specific to the hemolymph, CP2, 3 and 4, were different from CP egg in mobility by PAGE, pI and peptide mapping profiles.
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