AFFINITY PURIFICATION AND PROPERTIES OF POLYPHENOLOXIDASE FROM SOLANUM-TUBEROSUM

Citation
Su. Pathak et Vs. Ghole, AFFINITY PURIFICATION AND PROPERTIES OF POLYPHENOLOXIDASE FROM SOLANUM-TUBEROSUM, Phytochemistry, 36(5), 1994, pp. 1165-1167
Citations number
18
Categorie Soggetti
Plant Sciences
Journal title
ISSN journal
00319422
Volume
36
Issue
5
Year of publication
1994
Pages
1165 - 1167
Database
ISI
SICI code
0031-9422(1994)36:5<1165:APAPOP>2.0.ZU;2-J
Abstract
Polyphenoloxidase from potato tuber was purified to homogeneity in a s ingle step by affinity chromatography using p-aminophenyl acetic acid as a ligand coupled to Sepharose 4B by the divinylsulphone activation method. The purified enzyme was homogeneous on native and SDS-PAGE, in dicating the absence of multiple forms of the enzyme. Spectroscopic st udies of the purified enzyme indicated a peak at 275 nm and a broad sh oulder in the region between 320 and 340 nm, which is a characteristic of a purified preparation. The M(r) was 60 x 10(3). The kinetics of t he purified enzyme were studied.