Isolation and Characterization of Patatin Isoforms

Patatin has, so far, been considered a homogeneous group of proteins. A comparison of the isoforms in terms of structural properties or stability has not been reported. A method to obtain various isoform fractions as well as a comparison of the physicochemical properties of these pools is presented....

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Bibliographic Details
Published in:Journal of agricultural and food chemistry 1999-11, Vol.47 (11), p.4587-4592
Main Authors: Pots, André M, Gruppen, Harry, Hessing, Martin, van Boekel, Martinus A. J. S, Voragen, Alphons G. J
Format: Article
Language:English
Subjects:
Animal, plant, fungal and microbial proteins, edible seaweeds and food yeasts
biochemical polymorphism
Biological and medical sciences
carbohydrates
Carboxylic Ester Hydrolases
chemical composition
Chromatography, High Pressure Liquid
Circular Dichroism
electrokinetic potential
Food Chemistry and Microbiology
Food industries
Fundamental and applied biological sciences. Psychology
Geïntegreerde levensmiddelentechnologie en -fysica
glycoproteins
heat stability
Integrated Food Science and Food Physics
Levensmiddelenchemie en -microbiologie
molecular weight
plant proteins
Plant Proteins - chemistry
Plant Proteins - isolation & purification
potatoes
Protein Conformation
Protein Folding
Solanum tuberosum
spectral analysis
Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
Temperature
tubers
VLAG
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Summary:Patatin has, so far, been considered a homogeneous group of proteins. A comparison of the isoforms in terms of structural properties or stability has not been reported. A method to obtain various isoform fractions as well as a comparison of the physicochemical properties of these pools is presented. Patatin could be separated in four isoform pools, denoted A, B, C, and D, representing 62%, 26%, 5%, and 7% of the total amount of patatin, respectively. These isoforms differed in surface charge, resulting in a different behavior on anion exchange chromatography, isoelectric focusing, native polyacrylamide gel, and capillary electrophoresis. All isoforms of the patatin family contained proteins with two molecular masses of approximately 40.3 and 41.6 kDa, respectively. The size of this difference in the molar mass (1300 Da) is on the order of one carbohydrate moiety. Despite the biochemical differences given above, no variations in the structural properties nor in the thermal conformational stability could be observed using far-ultraviolet circular dichroism, infrared, and fluorescence spectroscopy. Keywords: Patatin isoforms; isolation; characterization
ISSN:0021-8561
1520-5118
DOI:10.1021/jf981180n