Sulfhydryl-reagent inhibition of olfaction in a moth and effects of exposure to pheromone compounds or a pheromone analogue

1994 ◽  
Vol 19 (2) ◽  
pp. 185-194 ◽  
Author(s):  
Michel Renou ◽  
Sandrine Brousset
Keyword(s):  
Sulfhydryl Reagent ◽  
Pheromone Analogue

scholarly journals N-(3-Pyrene)maleimide: a Long Lifetime Fluorescent Sulfhydryl Reagent

1973 ◽  
Vol 248 (9) ◽  
pp. 3173-3177
Author(s):  
Joel K. Weltman ◽  
Robert P. Szaro ◽  
A. Raymond Frackelton ◽  
Robert M. Dowben ◽  
James R. Bunting ◽  
...  
Keyword(s):  
Sulfhydryl Reagent ◽  
Long Lifetime

Synthesis of a biologically active isomer of frontalin and some new products from acylative decarboxylation of 3-methyltricarballylic acid

1990 ◽  
Vol 68 (5) ◽  
pp. 782-786 ◽  
Author(s):  
George M. Strunz ◽  
Chao-Mei Yu ◽  
Li Ya ◽  
Peter S. White ◽  
E. A. Dixon
Keyword(s):  
Acetic Anhydride ◽  
Functional Groups ◽  
Bark Beetles ◽  
New Products ◽  
Major Product ◽  
Biologically Active ◽  
Catalysed Reaction ◽  
Active Isomer ◽  
Pheromone Analogue ◽  
Simple Manipulation

2-Acetonyl-2-methylsuccinic anhydride, 3, the major product from base-catalysed reaction of 3-methyltricarballylic acid with acetic anhydride, was converted by simple manipulation of functional groups into 1,5-dimethyl-2,7-dioxabicyclo[3.2.1]octane. This bicyclic ketal (6) is isomeric with frontalin, 7, an aggregation pheromone for Dendroctonus bark beetles. It elicited electroantennogram responses in D. ponderosae and D. rufipennis. Besides 3 and the known compounds, 4 and 5, two new minor products, 8 and 9, were identified from base-catalysed acylative decarboxylation of 3-methyltricarballylic acid. Keywords: pheromone analogue, Dendroctonus, bark beetles.

CHARACTERIZATION OF HUMAN OVARIAN OESTRADIOL-17β OXIDOREDUCTASE ACTIVITY

1977 ◽  
Vol 85 (3) ◽  
pp. 624-635 ◽  
Author(s):  
Donald E. Pittaway ◽  
Richard N. Andersen ◽  
James R. Givens
Keyword(s):  
Enzyme Activity ◽  
Enzyme Activities ◽  
Enzyme Preparation ◽  
Phenolic Hydroxyl ◽  
Supernatant Fraction ◽  
Oxidoreductase Activity ◽  
Sulfhydryl Reagent ◽  
Michaelis Constants ◽  
Human Ovaries

ABSTRACT Oestradiol-17β oxidoreductase activity, which catalyzes the interconversion of oestrone and oestradiol, was investigated in preparations of human ovaries. The enzyme activities were localized primarily in the 105 000 × g supernatant fraction; dialyzed supernatant preparations were used in subsequent studies. The pH optima were 6.9 for reduction and 8.1 for 17β-dehydrogenation. The apparent Michaelis constants for oestrone and oestradiol were 1 × 10-7 m and 5 × 10-7 m, respectively. The enzyme activity was present with either NADP(H) or NAD(H), though NADP(H) were the preferred cofactors. Non-aromatic steroids androstenedione, dehydroepiandrosterone, testosterone and 5-androstene-3β,17β-diol were poor substrates for the enzyme preparation. Methylation of the phenolic hydroxyl of oestrone and oestradiol resulted in slightly enhanced activities. The sulfhydryl reagent, N-ethylmaleimide, inhibited the reduction of oestrone. A dialyzed supernatant preparation retained approximately 79 % of the original enzyme activity when stored at −20°C for 6 weeks.

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