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Studies of the haemolymph and cuticular phenoloxidase in Spodoptera littoralis larvae
Year:
1972
Source of publication :
Insect Biochemistry
Authors :
Ishaaya, Isaac
;
.
Volume :
2
Co-Authors:
Ishaaya, I., Division of Entomology, The Volcani Center, Bet Dagan, Israel
Facilitators :
From page:
409
To page:
419
(
Total pages:
11
)
Abstract:
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.
Note:
Related Files :
acetone
Alcohols
Chelating Agents
enzyme inhibition
haemolymph phenoloxidase
optimum pH
Show More
Related Content
More details
DOI :
10.1016/0020-1790(72)90021-2
Article number:
Affiliations:
Database:
Scopus
Publication Type:
article
;
.
Language:
English
Editors' remarks:
ID:
21786
Last updated date:
02/03/2022 17:27
Creation date:
16/04/2018 23:46
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Scientific Publication
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
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