Purification and Some Properties of Rat Intestinal Ornithine Decarboxylase

Ornithine decarboxylase (ODC) was induced in rat small intestine by treatment with hypotonic solution in vitro and purified by two procedures, a conventional procedure and an immunoaffinity procedure. SDS-polyacrylamide gel electrophoresis showed that the molecular weight of the preparation purified...

Full description

Saved in:
Bibliographic Details
Published in:Journal of biochemistry (Tokyo) 1989-07, Vol.106 (1), p.167-171
Main Authors: Miyamoto, Ken-ichi, Oka, Tatsuzo, Fujii, Takeru, Yamaji, Masahiro, Minami, Hisanori, Nakabou, Yukihiro, Hagihira, Hiroshi
Format: Article
Language:English
Subjects:
Analytical, structural and metabolic biochemistry
Animals
Biological and medical sciences
Chemical Fractionation
Chemical Phenomena
Chemistry
Chromatography - methods
Eflornithine - metabolism
Electrophoresis, Polyacrylamide Gel - methods
Enzymes and enzyme inhibitors
Fundamental and applied biological sciences. Psychology
Hypotonic Solutions
Immunoenzyme Techniques
intestine
Intestine, Small - enzymology
Isoelectric Point
Lyases
Male
Mice
Molecular Weight
Ornithine Decarboxylase - isolation & purification
Protease Inhibitors - pharmacology
Rats
Rats, Inbred Strains
Tritium
Citations: Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:Ornithine decarboxylase (ODC) was induced in rat small intestine by treatment with hypotonic solution in vitro and purified by two procedures, a conventional procedure and an immunoaffinity procedure. SDS-polyacrylamide gel electrophoresis showed that the molecular weight of the preparation purified by the immunoaffinity procedure (Mr = 53, 000) was slightly larger than that of the preparation obtained by the conventional procedure (Mr-52, 000). Values for the Km for L-ornithine (0.1 mM), the isoelectric point (5.4), and the final specific activity (5.1–5.5 xlO5 nmol CO2/mg protein/30 min) of the two preparations were similar to those reported for the rat liver ODC. Addition of a protease inhibitor (limabean trypsin inhibitor) to the crude extract prevented the appearance of the smaller enzyme (Mr = 52, 000) obtained by the conventional purification procedure. Our result indicates that the large enzyme is native ODC and the smaller one is a partial proteolysis product of native ODC.
ISSN:0021-924X
1756-2651
DOI:10.1093/oxfordjournals.jbchem.a122808