נגישות
menu      
חיפוש מתקדם
Insect Biochemistry
Ishaaya, I., Division of Entomology, The Volcani Center, Bet Dagan, Israel
Active phenoloxidase was isolated from the larval haemolymph and cuticle. The activity of the haemolymph enzyme was very low, reaching only about 10 per cent of that of the cuticle. Proteolytic enzymes, acetone, and alcohols inhibited cuticle and haemolymph phenoloxidase to various extents. Potassium cyanide and sodium thiosulphate suppressed strongly the cuticle phenoloxidase; sodium azide and sodium chloride affected the enzyme activity to a much lesser degree. Chelating agents, such as sodium diethyldithiocarbamate, 2,3-dimercapto-propanol, d-penicillamine, and 8-hydroxyquinoline, inhibited strongly the phenoloxidase activity. Sodium diethyldithiocarbamate was the most effective compound, suppressing the enzyme activity at a concentration of 10-6-10-8 M. Its activity seems to result from tying up the active center(s) of the enzyme, and then blocking the substrate reaction. © 1972.
פותח על ידי קלירמאש פתרונות בע"מ -
הספר "אוצר וולקני"
אודות
תנאי שימוש
Studies of the haemolymph and cuticular phenoloxidase in Spodoptera littoralis larvae
2
Ishaaya, I., Division of Entomology, The Volcani Center, Bet Dagan, Israel
Studies of the haemolymph and cuticular phenoloxidase in Spodoptera littoralis larvae
Active phenoloxidase was isolated from the larval haemolymph and cuticle. The activity of the haemolymph enzyme was very low, reaching only about 10 per cent of that of the cuticle. Proteolytic enzymes, acetone, and alcohols inhibited cuticle and haemolymph phenoloxidase to various extents. Potassium cyanide and sodium thiosulphate suppressed strongly the cuticle phenoloxidase; sodium azide and sodium chloride affected the enzyme activity to a much lesser degree. Chelating agents, such as sodium diethyldithiocarbamate, 2,3-dimercapto-propanol, d-penicillamine, and 8-hydroxyquinoline, inhibited strongly the phenoloxidase activity. Sodium diethyldithiocarbamate was the most effective compound, suppressing the enzyme activity at a concentration of 10-6-10-8 M. Its activity seems to result from tying up the active center(s) of the enzyme, and then blocking the substrate reaction. © 1972.
Scientific Publication
You may also be interested in