作者: Kiyoshi KONDO , Hajime FUJIO , Tsunehisa AMANO
DOI: 10.1093/OXFORDJOURNALS.JBCHEM.A133729
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摘要: Three lysozymes (DLs-1, -2, and -3) were purified from Peking-duck egg white by adsorption on CM-Sephadex C-25 resin, followed Sephadex G-50 column chromatographies. The three enzymes each moved as a single band, but showed different electrophoretic mobilities, disc-polyacrylamide gel electrophoresis at pH 4.1. Final yields of DL-1, DL-2, DL-3 18.2%, 22.0%, 6.0%, respectively, the crude material adsorbed resin. enzymatic activities 1.53, 1.52, 1.34 times that hen lysozyme, using Micrococcus lysodeikticus cell wall substrate 6.2 37 degrees C. All DLs lacked histidine their amino acid compositions differed other few exchanges. sequences DL-2 DL-1 two displacements (Ser-37 to Gly Gly-71 Arg) (Pro-79 Arg in addition same substitutions), respectively. In comparison with Duck II III Kaki-duck (Hermann Jolles (1970) Biochim. Biophys. Acta 200, 178-179; Hermann et al. (1971) Eur. J. Biochem. 24, 12-17) regards sequences, is identical except for one displacement Gln-57 Glu II, while rather our lysozymes. gave precipitin lines any rabbit antisera against line fused completely Ouchterlony double diffusion tests. However, radiobinding inhibition assay some anti-DL clearly discriminated fine differences among DLs. residue 79 (Pro equilibrium clearest immunological difference kinds found