Purification and characterization of histidine decarboxylase from mouse kidney.
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.
D000818:Animals; D001665:Binding Sites; D002262:Carboxy-Lyases / Q000302:isolation & purification*; D004591:Electrophoresis, Polyacrylamide Gel; D005260:Female; D006640:Histidine Decarboxylase / Q000302:isolation & purification*; D007526:Isoelectric Point; D007668:Kidney / Q000187:drug effects / Q000201:enzymology*; D051379:Mice; D008810:Mice, Inbred C57BL; D008970:Molecular Weight; D013974:Thyroxine / Q000494:pharmacology
D002262:Carboxy-Lyases; D006640:Histidine Decarboxylase; D013974:Thyroxine