Investigations on the polymorphism of sperm diaphorase in man

Kühnl, P.; Langanke, U.; Spielmann, W.; Neubauer, M.

doi:10.1007/bf00280833

Cited by 20 publications

(3 citation statements)

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“…PAGIF methods have been successfully applied for subtyping different genetic mark ers such as «,-antitrypsin (PiM1>M2) [5], phosphoglucomutase (PGMxal-a4) [9], and sperm diaphorase (SD13) [10], The investigation of the Gc polymor phism by PAGIF in the pH range 4-6 per mits the determination of two common subtypes of Gc1. From our experience the differ entiation on fixed, unstained gels is easier than after staining with Coomassie brillant blue R 250; the unstained Gc bands contrast well against the background of other proteins in this area.…”

Section: Discussionmentioning

confidence: 99%

An Improved Method for the Identification of Gc1 Subtypes (Group-Specific Component) by Isoelectric Focusing

Kühnb¹,

Spielmann²,

Loa³

1978

Vox Sanguinis

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The occurrence of common subtypes of the Gc^1 gene in a German population (n = 261) was investigated by isoelectric focusing on thin layers of polyacrylamide in the pH range 4-6. Six common phenotypes designated Gc IS, IF, 1F-1S, 2-1S, 2-1F, and 2 are considered as gene products of three common alleles with the following frequencies: Gc^1 = 0.603, Gc^1F = 0.125, and Gc^2 = 0.272. The sum of the allele frequencies of Gcls and G^1F corresponds with that of the ‘old’ Gc1 allele. Family investigations are in agreement with an autosomal codominant way of inheritance. The method employed provides an identification of the subtypes within 4 h without using anti-Gc-serum for immunoprécipitation.

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Section: Discussionmentioning

confidence: 99%

An Improved Method for the Identification of Gc1 Subtypes (Group-Specific Component) by Isoelectric Focusing

Kühnb¹,

Spielmann²,

Loa³

1978

Vox Sanguinis

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“…The studies concerning diaphorases in spermatozoa have dealt mainly with their characterization in humans (Caldwell et al -1976;Kopetz et al -1979;Kuhnl et al -1977).…”

Section: Introductionmentioning

confidence: 99%

Activity and Localization of NADH-dependant Oxidoreductase (Diaphorase) in Boar Spermatozoa

2009

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Investigations were carried out into the activity and localization of NADHdependant 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-O,36U/mI and 0,26U/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. Aktivitat und Lokalisation von NADH-abhangiger Oxydoreduktase (Diaphorase) in EberspermatozoenZusammenfassung: Die Aktivitat der NADH-abhangigen Diaphorase wurde in Spermatozoen von Ebern untersucht. Das Ejakulat hierfiir wurde von gesunden Ebern gesammelt, die im A.I.Zentrum gehalten wurden. Die Extraktion des Enzyms erfolgte mit destilliertem Wasser und Triton X-100. Dabei ergab sich, dab zwei verschiedene Formen der Diaphorase gefunden werden konnten und zwar wasserloslich und Triton X-100 loslich, die eine niedrige Aktivitat ( -0,36U/ml und 0,26U/ml) aufwieseu. Das Enzym war in den Mitochondrien lokalisiert und bewirkte eine verschiedene Reaktionsintensitat zwischen den Spermazellen im selben Ejakulat. Es fand sich, dab ein Teil der Mitochondrien und der auSeren Hullen eine positive Reaktion zeigten. Es ist wahrscheinlich, daS das Enzym die Relation zwischen reduzierter und oxidierter Form der NADH reguliert, bei der Energiebalance und moglicherweise auch beim Mechanismus der Samenbeweglichkeit eine Rolle spielt.

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“…They are investigated mainly in human sperm, where several phenotypes are established (Caldwell et al, 1976;Edwards et al, 1979;Kido et al, 1987;Kopetz et al. 1979;Kuhnl et al, 1977;Sebatan et al, 1982). However, not enough data are available for spermatozoa diaphorases in other mammals (Hrudka, 1979).…”

Section: Introductionmentioning

confidence: 99%

Electrophoresis of NADH-dependent oxidoreductase (diaphorase) in boar spermatozoa: Elektrophorese der NADH-abhängigen Oxydoreduktase (Diaphorase) in Eberspermatozoen

Atanassov

Georgiev

2009

Andrologia

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Two forms of NADH-dependent oxidoreductase (diaphorase rEC.1.6.99.-1) are established in boar spermatozoa. The first form is typical for soluble proteins with a varying electrophoretic profile, while the other form for sedimental proteins with a specific, slowlymoving fraction, which is not common for the soluble form. The two enzyme forms have a close isoelectric point (PI 5.5-6.0) and they can not be inhibited by dicumarol moll-' and FAD moll-'. The molecular mass of the soluble form of the enzyme is 28,37,46 and 67 kD, while of the sedimental form it is 220, 250 and 260 kD, respectively.Zusammenfassung. In Eberspermatozoen sind zwei Formen der NADH-abhangigen Oxydoreduktase (Diaphorase rEC.1.6.99.-1) vorhanden. Die erste Form ist typisch fur losliche Proteine mit einem unterschiedlichen elektrophoretischen Profil, die andere Form fur Sediment-Proteine mit einer spezifischen, langsam wandernden Fraktion, die nicht ublich ist fur die losliche Form. Die beiden Enzyme haben einen nahe beieinander liegenden isoelektrischen Punkt (PI 5,s-6,O); sie konnen nicht durch Dicumarol mol-' und FAD mol-' gehemmt werden. Das Molekulargewicht der loslichen Form des Enzyms ist 28, 37,46 und 67 kD, wahrend dieses fur die Sediment-Form 220,250 und 260 kD betragt. In memoriam:Professor Tapani Vanha-Perttula, Professor and Chairman of Anatomy, University of Kuopio, and the former Rector of the University of Kuopio, was killed in a traffic accident with an elk on February 11, 1990, in Kuopio.Tapani Vanha-Perttula was very successful in his research activities. He published more than 140 original full length papers. He also investigated the presence of trace elements in the seminal plasma and in the sperms and the effect of these elements on fertilization as well as the effects of enzyme inhibitors on the maturation of sperms and their fertilizing ability.The Editors of andrologia lost a very good friend; he published many excellent papers and served as a referee for our journal.androloPia 22. No. 6 (1990)

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Investigations on the polymorphism of sperm diaphorase in man

Cited by 20 publications

References 12 publications

An Improved Method for the Identification of Gc1 Subtypes (Group-Specific Component) by Isoelectric Focusing

An Improved Method for the Identification of Gc1 Subtypes (Group-Specific Component) by Isoelectric Focusing

Activity and Localization of NADH-dependant Oxidoreductase (Diaphorase) in Boar Spermatozoa

Electrophoresis of NADH-dependent oxidoreductase (diaphorase) in boar spermatozoa: Elektrophorese der NADH-abhängigen Oxydoreduktase (Diaphorase) in Eberspermatozoen

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