Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
1987-11-17
pubmed:abstractText
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.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0303-4569
pubmed:author
pubmed:issnType
Print
pubmed:volume
19
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
474-7
pubmed:dateRevised
2003-11-14
pubmed:meshHeading
pubmed:articleTitle
Activity and localization of NADH-dependant oxidoreductase (diaphorase) in boar spermatozoa.
pubmed:affiliation
Institute of Biology and Immunology of Reproduction, Bulgarian Academy of Sciences, Sofia.
pubmed:publicationType
Journal Article