作者: R. Marzocchini , G. Camici , G. Ramponi , D. Degl'Innocenti , A. Berti
DOI: 10.1007/BF00276734
关键词:
摘要: The main antibody-combining sites of horse skeletal muscle acylphosphatase were mapped by preparing and purifying CNBr, tryptic peptic peptides from the pure enzyme, looking for immunoreactivity each peptide dot-immunobinding assay using specific polyclonal antienzyme antibodies previously purified immunoaffinity chromatography. immunoreactive identified on basis either their elution times in fingerprint analysis or amino acid composition, both, comparison with known enzyme sequence. All CNBr as well two immunopositive, leading to identification three continuous antigenic molecule. strong inhibition (92%) antigen-antibody reaction carried out presence incubated mixture supports possibility that, at our experimental condition, domains contain determinants enzyme. relationship between structure antigenicity is discussed detail.