Characterization of nonheme type bromoperoxidase in Corallina pilulifera.
作者： N Itoh , Y Izumi , H Yamada
DOI: 10.1016/S0021-9258(19)89233-5
关键词: Vanadium bromoperoxidase 、 Molecular mass 、 Electrophoreses 、 Biochemistry 、 Isoelectric point 、 Enzyme 、 Amino acid 、 Chemistry 、 Bromoperoxidase 、 Hemeprotein 、 Stereochemistry
摘要: Bromoperoxidase was purified from the crude extract of Corallina pilulifera to be homogeneous upon polyacrylamide disc gel and sodium dodecyl sulfate-polyacrylamide electrophoreses according procedures previously reported (Itoh, N., Izumi, Y., Yamada, H. (1985) Biochem. Biophys. Res. Commun. 131, 428-435). The enzyme had a molecular weight approximately 790,000 composed 12 subunits identical weights (Mr 64,000). Hexagonal shapes were observed by electron microscopy. isoelectric point 3.0, predominance acidic amino acids revealed acid analysis enzyme. specific for I- Br- inactive toward Cl- F-. optimum pH 6.0, stable in range 5.0 11.0. no hemeor flavin-like compounds as prosthetic group. Plasma emission spectroscopy that contains 2.3 +/- 0.2 atoms iron 1.6 0.1 magnesium/molecule protein. Hence, bromoperoxidase C. distinct other haloperoxidases many peroxidases, which are hemoproteins.
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