Format

Send to

Choose Destination
Biochem J. 1973 Feb;131(2):187-90.

Characterization of alternative molecular forms of xanthine oxidase in the mouse.

Abstract

1. Two major forms of xanthine oxidase are demonstrated for the mouse. On polyacrylamide-gel electrophoresis the duodenal form migrates faster towards the anode than that of the liver. Both forms also differ in their (NH(4))(2)SO(4) precipitation patterns and sucrose-density-gradient molecular-weight determinations. 2. The liver form is fully converted into the duodenal form by incubation at 37 degrees C with 2.5mg of crude trypsin/ml for 1(1/2)h, without loss of activity. The trypsin-treated liver form behaves like the normal duodenal form as characterized by electrophoresis, (NH(4))(2)SO(4) precipitation patterns, and sucrose-density-gradient molecular-weight determinations. 3. Partial conversion is also brought about by purified trypsin and chymotrypsin, but not with beta-carboxypeptidase or lipase. The conversion is inhibited by soya-bean trypsin inhibitor. 4. In embryo mice the duodenal form is similar to the liver form on electrophoresis. 5. These studies indicate, as might be expected, that the duodenal form is a modified version of the liver enzyme, probably caused by proteolytic alteration.

PMID:
4722435
PMCID:
PMC1177457
DOI:
10.1042/bj1310187
[Indexed for MEDLINE]
Free PMC Article

Supplemental Content

Full text links

Icon for HighWire Icon for PubMed Central
Loading ...
Support Center