Access the full text.
Sign up today, get DeepDyve free for 14 days.
S. Shaltiel (1974)
[9] Hydrophobic chromatographyMethods in Enzymology, 34
Demetri Kokkinakis, James Brooks (1979)
Tomato peroxidase: purification, characterization, and catalytic properties.Plant physiology, 63 1
Jen Jen, Flurkey Flurkey (1979)
Hydrophobic chromatography of peach fruit polyphenol oxidaseHortScience, 14
J. Evans (1968)
Peroxidases from the extreme dwarf tomato plant. Identification, isolation, and partial purification.Plant physiology, 43 7
A. Signoret, J. Crouzet (1978)
トマト果実におけるポリフェノールオキシダーゼおよびペルオキシダーゼ活性 精製とその性質 | 文献情報 | J-GLOBAL 科学技術総合リンクセンター, 42
W. Flurkey, Linda Young, J. Jen (1978)
Separation of soybean lipoxygenase and peroxidase by hydrophobic chromatographyJournal of Agricultural and Food Chemistry, 26
Flurkey Flurkey, Young Young, Jen Jen (1978)
Separation of Soybean lipooxygenase and peroxidase activities by hydrophobic chromatographyJ. Agric. Food Chem, 26
J. Evans (1970)
Spectral similarities and kinetic differences of two tomato plant peroxidase isoenzymes.Plant physiology, 45 1
Hoyle Hoyle (1978)
High resolution of peroxidase‐IAA oxidase isoenzymes from horseradish by isoelectric focusingPlant Physiol, 60
W. Flurkey, J. Jen (1978)
PEROXIDASE AND POLYPHENOL OXIDASE ACTIVITIES IN DEVELOPING PEACHESJournal of Food Science, 43
K. Weber, M. Osborn (1969)
The reliability of molecular weight determinations by dodecyl sulfate-polyacrylamide gel electrophoresis.The Journal of biological chemistry, 244 16
U. Laemmli (1970)
Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 227
F. Burnette (1977)
PEROXIDASE AND ITS RELATIONSHIP TO FOOD FLAVOR AND QUALITY: A REVIEWJournal of Food Science, 42
D. Kokkinakis, J. Brooks (1979)
Hydrogen Peroxide-mediated Oxidation of Indole-3-acetic Acid by Tomato Peroxidase and Molecular Oxygen.Plant physiology, 64 2
Merrill Hoyle (1977)
High resolution of peroxidase-indoleacetic Acid oxidase isoenzymes from horseradish by isoelectric focusing.Plant physiology, 60 5
Ann Huang, N. Haard (1977)
PROPERTIES OF IAA OXIDASE FROM RIPENING TOMATO FRUITJournal of Food Biochemistry, 1
Signoret Signoret, Crouzet Crouzet (1978)
Activities of polyphenol oxidase and peroxidase in tomato fruitAgric. Biol. Chem, 42
John Evans, N. Alldridge (1965)
The distribution of peroxidases in extreme dwarf and normal tomato (Lycopersicon Esculentum Mill.)Phytochemistry, 4
A. Signoret, J. Crouzet (1978)
Activités Polyphénoloxydasique et Peroxydasique du Fruit de la Tomate (Lycopersicum esculentum) Purification et Quelques PropriétésAgricultural and biological chemistry, 42
ABSTRACT With a large number of isoenzyme species and substrates, peroxidases have been difficult to purify to homogeneity. By including hydrophobic chromatography in the purification scheme, a homogeneous tomato fruit peroxidase isoenzyme was obtained. The isoenzyme had a clean spectrum in the visible region and a Rz (403 nm/280 nm) value of 2.36. It showed up as a single band in disc gel electrophoresis in basic and acidic buffers, in acetate strip electrophoresis, and in both tube and slab gel SDS electrophoresis. Molecular weight estimation of this tomato peroxidase was 43,000 ± 2,000 daltons. The pH optima were at 5.5 and 7.5 with guaiacol and pyrogallol as substrate, respectively. Kinetic studies showed that pyrogallol and hydrogen peroxide could provide substrate inhibition at 5 mM concentration. Hydrophobic chromatography may be useful for purification of other food enzymes similar to tomato peroxidase.
Journal of Food Science – Wiley
Published: Jan 1, 1980
Read and print from thousands of top scholarly journals.
Already have an account? Log in
Bookmark this article. You can see your Bookmarks on your DeepDyve Library.
To save an article, log in first, or sign up for a DeepDyve account if you don’t already have one.
Copy and paste the desired citation format or use the link below to download a file formatted for EndNote
Access the full text.
Sign up today, get DeepDyve free for 14 days.
All DeepDyve websites use cookies to improve your online experience. They were placed on your computer when you launched this website. You can change your cookie settings through your browser.