title: Resonance Raman characterization of hog thyroid peroxidase. An SERRS study.
abstract: Resonance Raman (RR) spectra of hog thyroid peroxidase (TPO) were observed for the first time and compared with those of lactoperoxidase (LPO) and horseradish peroxidase (HRP). Since TPO purified by monoclonal antibody-assisted immunoaffinity chromatography was strongly fluorescent, the surface enhancement technique using Ag colloid adsorption was used for the oxidized form, but ordinary RR spectra could be obtained for the reduced form. The RR spectra of TPO were distinct from those of HRP in both the oxidized and reduced states and indicated the presence of six-coordinated iron-protoporphyrin.
authors.affiliation: Institute for Molecular Science, Okazaki National Research Institutes, Japan.
authors.forename: S
authors.initials: S
authors.lastname: Hashimoto
authors.forename: R
authors.initials: R
authors.lastname: Nakajima
authors.forename: I
authors.initials: I
authors.lastname: Yamazaki
authors.forename: T
authors.initials: T
authors.lastname: Kotani
authors.forename: S
authors.initials: S
authors.lastname: Ohtaki
authors.forename: T
authors.initials: T
authors.lastname: Kitagawa
mesh_terms: D000818:Animals; D000911:Antibodies, Monoclonal; D002846:Chromatography, Affinity; D006735:Horseradish Peroxidase / Q000032:analysis; D007453:Iodide Peroxidase / Q000032:analysis*; D007784:Lactoperoxidase / Q000032:analysis; D010084:Oxidation-Reduction; D013050:Spectrometry, Fluorescence; D013552:Swine
chemical_list: D000911:Antibodies, Monoclonal; D006735:Horseradish Peroxidase; D007784:Lactoperoxidase; D007453:Iodide Peroxidase