Two immunologically different isozymes of ascorbate peroxidase from spinach leaves.
Two isozymes of ascorbate peroxidase (AP) from spinach leaves were separated by hydrophobic chromatography and designated AP-I and AP-II. They had similar molecular weights of about 31,000, as determined by gel-filtration, and showed high specificity for ascorbate. One of the two isozymes (AP-II) was purified to homogeneity by SDS-PAGE. Immunoblotting confirmed that antiserum against AP-II reacted with AP-II but not with AP-I. This antiserum inhibited the activity of AP-II, but not that of AP-I. The amino acid composition and partial amino acid sequence of AP-II were determined.
Tanaka
K
K
Division of Environmental Biology, National Institute for Environmental Studies, Ibaraki, Japan.
Takeuchi
E
E
Kubo
A
A
Sakaki
T
T
Haraguchi
K
K
Kawamura
Y
Y
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D060387:Ascorbate Peroxidases; D002736:Chloroplasts / Q000201:enzymology; D004591:Electrophoresis, Polyacrylamide Gel; D007106:Immune Sera; D015151:Immunoblotting; D007527:Isoenzymes / Q000276:immunology / Q000302:isolation & purification*; D008969:Molecular Sequence Data; D008970:Molecular Weight; D010544:Peroxidases / Q000276:immunology / Q000302:isolation & purification*; D010944:Plants / Q000201:enzymology*
D000596:Amino Acids; D007106:Immune Sera; D007527:Isoenzymes; D010544:Peroxidases; D060387:Ascorbate Peroxidases