1. Purification and characterization of histidine decarboxylase from mouse kidney
- Author
-
J O Bishop and S A M Martin
- Subjects
Carboxy-Lyases ,Protein subunit ,Size-exclusion chromatography ,Fractionation ,Histidine Decarboxylase ,Kidney ,Biochemistry ,Mice ,Column chromatography ,Animals ,Isoelectric Point ,Molecular Biology ,Gel electrophoresis ,chemistry.chemical_classification ,Binding Sites ,Chromatography ,Chemistry ,Chromatofocusing ,Cell Biology ,Histidine decarboxylase ,Mice, Inbred C57BL ,Molecular Weight ,Thyroxine ,Enzyme ,Electrophoresis, Polyacrylamide Gel ,Female ,Research Article - Abstract
Histidine decarboxylase was purified 800-fold from the kidneys of thyroxine-treated mice. The purification procedure included precipitation of protein from a crude supernatant after heating it to 55 degrees C at pH 5.5, fractionation with (NH4)2SO4, phosphocellulose column chromatography, chromatofocusing, DEAE-Sepharose column chromatography, gel filtration on Sephacryl S-300 and preparative polyacrylamide-gel electrophoresis. The native enzyme had an estimated Mr of 113 000. The protein was analysed in SDS/10%-polyacrylamide gels and formed a single band corresponding to a subunit Mr of 55 000, indicating that it is a dimer. Three forms of the enzyme were resolved on isoelectrofocusing gels, with pI 5.3, 5.5 and 5.7.
- Published
- 1986
- Full Text
- View/download PDF