נגישות
menu      
חיפוש מתקדם
Phytochemistry
Ben-Shalom, N., Division of Food Technology, Agricultural Research Organization, The Volcani Center, Bet Dagan, Israel
Kahn, V., Division of Food Technology, Agricultural Research Organization, The Volcani Center, Bet Dagan, Israel
Harel, E., Botany Department, The Hebrew University of Jerusalem, Israel
Mayer, A.M., Botany Department, The Hebrew University of Jerusalem, Israel
Catechol oxidase was extracted from an acetone powder prepared from green olive. The enzyme was purified 240-fold by ammonium sulphate fractionation followed by ion exchange chromatography and gel filtration. The enzyme was characterized by substrate specificity and response to inhibitors. Between 7 and 9 bands having catechol oxidase activity could be detected by gel electrophoresis and electrofocusing. The purified enzyme had an estimated MW of 42 000. The enzyme was strongly inhibited by diethyldithiocarbamate. Inhibition by chloride was strongly dependent on pH. The enzyme did not oxidise monophenols. © 1977.
פותח על ידי קלירמאש פתרונות בע"מ -
הספר "אוצר וולקני"
אודות
תנאי שימוש
Catechol oxidase from green olives: Properties and partial purification
16
Ben-Shalom, N., Division of Food Technology, Agricultural Research Organization, The Volcani Center, Bet Dagan, Israel
Kahn, V., Division of Food Technology, Agricultural Research Organization, The Volcani Center, Bet Dagan, Israel
Harel, E., Botany Department, The Hebrew University of Jerusalem, Israel
Mayer, A.M., Botany Department, The Hebrew University of Jerusalem, Israel
Catechol oxidase from green olives: Properties and partial purification
Catechol oxidase was extracted from an acetone powder prepared from green olive. The enzyme was purified 240-fold by ammonium sulphate fractionation followed by ion exchange chromatography and gel filtration. The enzyme was characterized by substrate specificity and response to inhibitors. Between 7 and 9 bands having catechol oxidase activity could be detected by gel electrophoresis and electrofocusing. The purified enzyme had an estimated MW of 42 000. The enzyme was strongly inhibited by diethyldithiocarbamate. Inhibition by chloride was strongly dependent on pH. The enzyme did not oxidise monophenols. © 1977.
Scientific Publication
You may also be interested in