A non-penetrating thiol reagent mimics cytochalasin a inhibition of secretory protein synthesis

Mimicry of selective cytochalasin A (CA) inhibition of cellulase synthesis in the water mold Achlya by the non-penetrating thiol reagent, p-chloromercuribenzene sulphonate suggests that CA may act as a non-permeant sulphydryl reagent, and that inhibition of cellulase synthesis may be exerted via rel...

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Bibliographic Details
Published inBiochemical and biophysical research communications Vol. 71; no. 1; pp. 280 - 285
Main Authors Manavathu, Elias K., Thomas, Donovan des S.
Format Journal Article
LanguageEnglish
Published United States Elsevier Inc 01.01.1976
Subjects
Benzenesulfonates - pharmacology
Binding Sites
Cellulase - biosynthesis
Cycloheximide - pharmacology
Cytochalasins - pharmacology
Enzyme Induction - drug effects
Ethylmaleimide - pharmacology
Fungi - drug effects
Fungi - metabolism
Glutathione - pharmacology
Kinetics
Myxomycetes
Protein Biosynthesis - drug effects
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Summary:Mimicry of selective cytochalasin A (CA) inhibition of cellulase synthesis in the water mold Achlya by the non-penetrating thiol reagent, p-chloromercuribenzene sulphonate suggests that CA may act as a non-permeant sulphydryl reagent, and that inhibition of cellulase synthesis may be exerted via relatively superficial thiol groups in the plasma membrane.
ISSN:0006-291X
1090-2104
DOI:10.1016/0006-291X(76)90279-5