Activity and localization of NADH-dependant oxidoreductase (diaphorase) in boar spermatozoa

Investigations were carried out into the activity and localization of NADH-dependant diaphorase in boar spermatozoa. Semen samples were collected from healthy boars, used in A.I. centers. The enzyme was extracted with distilled water and Triton X-100. Two forms of diaphorase were found-water-soluble...

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Bibliographic Details
Published in:Andrologia Vol. 19; no. 4; p. 474
Main Authors: Atanassov, B, Denkova, R, Georgiev, G
Format: Journal Article
Language:English
Published: Germany 01-07-1987
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Summary:Investigations were carried out into the activity and localization of NADH-dependant diaphorase in boar spermatozoa. Semen samples were collected from healthy boars, used in A.I. centers. The enzyme was extracted with distilled water and Triton X-100. Two forms of diaphorase were found-water-soluble and Triton X-100 soluble, showing low activity-0.36 U/ml and 0.26 U/ml. The enzyme was localized in the mitochondria, manifesting different intensities of reaction between sperm cells in the same ejaculate. It was found, that a part of the mitochondria and outer doublets showed positive reaction. It is suggested that the enzyme regulates the ratio between reduced and oxidized forms of NADH, takes part in the energy balance and possibly in the mechanism of sperm motility.
ISSN:0303-4569
DOI:10.1111/j.1439-0272.1987.tb02331.x