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Journal ArticleDOI

Epoxidation of aldrin by cell-free pea root preparations

P. C. Oloffs
- 01 Nov 1970 - 
- Vol. 1, Iss: 6, pp 228-232
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TLDR
The epoxidation of aldrin and factors influencing this reaction were studied with buffered, aqueous, cell-free preparations obtained from unbroken roots of laboratory-grown peas, indicating that the epoxidising factor was soluble, and not dependent on the presence of intact cells or cell organelles.
Abstract
The epoxidation of aldrin and factors influencing this reaction were studied with buffered, aqueous, cell-free preparations obtained from unbroken roots of laboratory-grown peas. Aldrin was available to the epoxidising enzymes at concentrations which far exceeded its reported water solubility. Under the experimental conditions, the optimum pH for the reaction was 6·5 using 0·02M phosphate buffer. The reaction rate increased up to 35°c, and decreased with higher temperatures. Various treatments indicated that the epoxidising factor was soluble, and not dependent on the presence of intact cells or cell organelles. No need could be shown for the cofactors NADPH2 and Mg2+, which are required for animal microsomal oxidations. Inhibitor studies indicated both differences and similarities between the system studied here and animal microsomal preparations.

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Citations
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Journal ArticleDOI

Oxidative Metabolism of Foreign Compounds by Higher Plants

TL;DR: In this article, the Oxidative Metabolism of Foreign Compounds of Higher Plants by Higher Plants is discussed. But they focus on higher plants and do not consider higher plants.
Journal ArticleDOI

Fate and behavior of five chlorinated hydrocarbons in three natural waters.

TL;DR: Water samples removed from two rivers and from the subtidal zone of Georgia Strait in British Columbia were treated with either 0.025 ppm of DDT, lindane, α- chlordane, or γ-chlordane to establish an experimental procedure to evaluate the phytochemical properties of these compounds.
Journal ArticleDOI

Aldrin epoxidation by plant root extracts

TL;DR: Aldrin epoxidase activity of the cell-free pea and bean root preparations was located in the particulate fraction and was increased by addition of p -aminobenzoic acid (10 −4 M).
Journal ArticleDOI

Residues in cutthroat trout (Salmo clarki) and California newts (Tarichia torosa) from a lake treated with technical chlordane.

TL;DR: The results strongly suggest that the California newt metabolizes and eliminates chlordane residues more effectively than the cutthroat trout.
References
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Journal ArticleDOI

Photochemical Action Spectrum of the Terminal Oxidase of Mixed Function Oxidase Systems

TL;DR: The agreement between photochemical action spectrum and spectrophotometric difference spectrum supports the conclusion that the CO-binding pigment is the terminal oxidase of mixed function oxidase systems of mammals.
Journal ArticleDOI

Microsomal epoxidation of cyclodiene insecticides.

TL;DR: Rabbit liver microsomes were shown to contain enzyme systems that converted heptachlor, aldrin, and isodrin into their corresponding epoxides, and mutual inhibition between the two substrates as well as inhibition by epoxide was observed.
Journal ArticleDOI

Hydrogenase of Clostridium butylicum.

TL;DR: The cell free hydrogenases of Clostridium butylicum and Micrococcus aerogenes are incapable of reducing commonly used two-electron dye acceptors such as methylene blue at appreciable rates in the presence of molecular hydrogen, while the crude and partially purified enzyme from numerous other sources reduces such dyes readily.
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