منابع مشابه
Studies of enzyme inhibition by compounds containing small rings.
Our interest in the enzyme chemistry of compounds containing small rings developed from a speculative study of the inhibition of alcohol dehydrogenase by allylic alcohols (MacInnes et al., 1981) in which we found that 3-thioethylprop-2-en1-01 (I) was a potent inhibitor of this enzyme. Our original strategy was that oxidation of (I) would lead to an a,/?-unsaturated aldehyde to which a nucleophi...
متن کاملENZYME INHIBITION BY HERBAL MOLLUSCICIDES IN THE NERVOUS TISSUE OF THE SNAIL LYMNAEA ACUMINATA
The effect of Annona squamosa, Lawsonia inermis and their combination with other herbal molluscicides were studied on different enzyme activity in the nervous tissue of Lymnaea acuminata. Twenty-Four hour in vivo exposure to 40% and 80% of 24 h LC50 of plant derived molluscicides and their combination with other molluscicides such as Cedrus deodara, Azadirachta indica oil, Allium sativum, Polia...
متن کاملInhibition of Cyclooxygenase Type 1 and 2 Enzyme by Aqueous Extract of Elaeagnus Angustifolia in Mice
Introduction: It has been shown that the extract of Elaeagnus angustifolia can inhibit inflammation and pain induced by formalin in mice and rats. The aim of the present study is to reach evaluations of possible cellular and molecular mechanisms of Elaeagnus angustifolia extract in reducing pain and inflammation through examining the extract ability for inhibition of cyclooxygenase (Cox) type ...
متن کاملInhibition of aflatoxin biosynthesis by phenolic compounds.
The phenolic compounds acetosyringone, syringaldehyde and sinapinic acid inhibited the biosynthesis of aflatoxin B1 (AFB1) by A. flavus. Acetosyringone was the most active among the three compounds, inhibiting aflatoxin level by 82% at 2 m moll-1. The synthesis and accumulation of norsolorinic acid, an aflatoxin biosynthetic intermediate, was also inhibited. These results suggest that at least ...
متن کاملCompetitive inhibition of enzyme activity by urea.
It is widely accepted that urea and guanidine act as protein denaturants by breaking intramolecular hydrogen bonds (1). Loss of catalytic activity in the presence of urea is thought to occur by elimination of bonds contributing to the tertiary structure of enzyme molecules. Subsequent restoration of structural and catalytic properties by removal of the denaturant, “reversible denaturation,” is ...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1990
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(17)44813-7