נגישות
menu      
Advanced Search
Syntax
Search...
Volcani treasures
About
Terms of use
Manage
Community:
אסיף מאגר המחקר החקלאי
Powered by ClearMash Solutions Ltd -
Phenyltin compounds inhibit digestive enzymes of Tribolium confusum larvae
Year:
1975
Authors :
Ishaaya, Isaac
;
.
Volume :
5
Co-Authors:
Ishaaya, I., Division of Entomology and Parasitology, University of California, Berkeley, CA 94720, United States
Casida, J.E., Division of Entomology and Parasitology, University of California, Berkeley, CA 94720, United States
Facilitators :
From page:
350
To page:
358
(
Total pages:
9
)
Abstract:
The potency of dietary phenyltin compounds in inhibiting the growth of first and fourth instar Tribolium confusum L. larvae and the gut proteolytic activity of fourth instar larvae decreases in the order of triphenyltin chloride (Ph3SnCl) ≫ diphenyltin dichloride (Ph2SnCl2) ≫ phenyltin trichloride or tetraphenyltin. The growth retardation, which prolongs the larval stage without affecting pupation or emergence, may result from an antifeeding effect involving gut protease inhibition by Ph3Sn+ and Ph2Sn2+. Gut amylase and invertase activities are less sensitive than the protease activity to in vivo inhibition. Under in vitro conditions, relatively high concentrations of Ph3SnCl and Ph2SnCl2 are required for inhibition, the order of enzyme sensitivity is protease > amylase > invertase, and Ph2SnCl2 is more potent than Ph3SnCl. Proteins such as casein, albumin and hemoglobin, but not carbohydrates such as starch and sucrose bind Ph3Sn+ so it is inaccessible for inhibition of digestive enzymes. The level of Ph3Sn+ inhibiting gut protease in vivo is far below that necessary for in vitro inhibition of this enzyme activity. It is speculated that the in vivo inhibitory effects of Ph3Sn+ and Ph2Sn2+ on digestive enzymes may result from binding to the enzyme protein, its zymogen or to other proteins involved in production of the digestive enzymes. © 1975.
Note:
Related Files :
amylase
enzyme inhibition
invertebrate
oral drug administration
Starch
sucrose
Tribolium confusum
water
Show More
Related Content
More details
DOI :
10.1016/0048-3575(75)90055-3
Article number:
Affiliations:
Database:
Scopus
Publication Type:
article
;
.
Language:
English
Editors' remarks:
ID:
21627
Last updated date:
02/03/2022 17:27
Creation date:
16/04/2018 23:45
You may also be interested in
Scientific Publication
Phenyltin compounds inhibit digestive enzymes of Tribolium confusum larvae
5
Ishaaya, I., Division of Entomology and Parasitology, University of California, Berkeley, CA 94720, United States
Casida, J.E., Division of Entomology and Parasitology, University of California, Berkeley, CA 94720, United States
Phenyltin compounds inhibit digestive enzymes of Tribolium confusum larvae
The potency of dietary phenyltin compounds in inhibiting the growth of first and fourth instar Tribolium confusum L. larvae and the gut proteolytic activity of fourth instar larvae decreases in the order of triphenyltin chloride (Ph3SnCl) ≫ diphenyltin dichloride (Ph2SnCl2) ≫ phenyltin trichloride or tetraphenyltin. The growth retardation, which prolongs the larval stage without affecting pupation or emergence, may result from an antifeeding effect involving gut protease inhibition by Ph3Sn+ and Ph2Sn2+. Gut amylase and invertase activities are less sensitive than the protease activity to in vivo inhibition. Under in vitro conditions, relatively high concentrations of Ph3SnCl and Ph2SnCl2 are required for inhibition, the order of enzyme sensitivity is protease > amylase > invertase, and Ph2SnCl2 is more potent than Ph3SnCl. Proteins such as casein, albumin and hemoglobin, but not carbohydrates such as starch and sucrose bind Ph3Sn+ so it is inaccessible for inhibition of digestive enzymes. The level of Ph3Sn+ inhibiting gut protease in vivo is far below that necessary for in vitro inhibition of this enzyme activity. It is speculated that the in vivo inhibitory effects of Ph3Sn+ and Ph2Sn2+ on digestive enzymes may result from binding to the enzyme protein, its zymogen or to other proteins involved in production of the digestive enzymes. © 1975.
Scientific Publication
You may also be interested in