Pyridine-Nucleotide Coenzymes in Bull and Rabbit Spermatozoa

Bistocchi, M; D’Alessio, Giuseppe; Leone, E

doi:10.1530/jrf.0.0160223

Cited by 16 publications

(11 citation statements)

References 5 publications

(7 reference statements)

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“…Bistocchi et al (1968) showed that ejaculated bull spermatazoa possessed less than 35 % of the levels of NAD and NADP found in epididymal spermatazoa. It has not been resolved whether NAD and NADP are hydrolysed by the same enzyme which cleaves the ribosyl pyridinium bond.…”

Section: Introd:uctionmentioning

confidence: 99%

Pyridine Nucleosidase in Bull Semen ll. Biochemical Properties

Giles¹,

Kl²

1975

Aust. Jnl. Of Bio. Sci.

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It is most likely a single enzyme (NAD+ nucleosidase) present in semen from most bulls which hydrolyses the ribosyl pyridinium bond in both NAD and NADP. This conclusion is based on the following results: (i) each of 12 semen samples containing nucleosidase activity hydrolysed NAD at the same rate as NADP (r = 0·99); (ii) other untreated semen samples from different bulls which did not hydrolyse NAD were also inactive against NADP; (iii) enzyme denaturation produced by preliminary heating of semen filtrates for 15 min at varied temperatures or by heating at 55°C for varied time intervals caused similar reductions in the rates of NAD and NADP hydrolysis; and (iv) nicotinamide inhibited enzyme activity to the same degree using either NAD or NADP as the substrate. Introd:uctionThe biological significance of a soluble pyridine nucleosidase in bull semen originally identified by Leone and Bonaduce (1959) has not been elucidated. Bistocchi et al. (1968) showed that ejaculated bull spermatazoa possessed less than 35 % of the levels of NAD and NADP found in epididymal spermatazoa. It has not been resolved whether NAD and NADP are hydrolysed by the same enzyme which cleaves the ribosyl pyridinium bond. Macmillan et al. (1975) found that the concentration of seminal pyridine nucleosidase varied between bulls from zero to 1470 enzyme unitsfml semen but only NAD was used as the enzyme substrate. This wide range in enzyme concentration facilitated studies to determine whether more than one pyridine nucleosidase was involved. Materials and MethodsThe procedures used for semen sampling .and storage, and for assaying nucleosidase activity have been reported previously (Macmillan et al. 1975).The effect of temperature on enzyme inactivation was assessed by heating 1 ml of the diluted semen filtrate for 15 min at 40, 45, 50, 55, 60 or 70°C followed by rapid cooling to 20°C. The rate of enzyme inactivation was measured by heating similar semen samples at 55°C for from 5 to 40 min.The effect on nicotinamide inhibition on enzyme activity was measured by adding from 0·39 to 100 mmol of nicotinamide in 0·05 ml volume to 1·0 ml ofthe semen filtrate prior to the addition of NAD or NADP. Standards for each concentration of nicotinamide to which neither NAD nor NADP was added were also incubated.• Part I, Aust. J. Bioi. Sci., 28, 267-72.

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Section: Introd:uctionmentioning

confidence: 99%

Pyridine Nucleosidase in Bull Semen ll. Biochemical Properties

Giles¹,

Kl²

1975

Aust. Jnl. Of Bio. Sci.

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“…Macmillan (1973) concluded that sire differences in conception rate primarily involved variation in the duration of post-insemination sperm liveability. Bistocchi et al (1968) showed that after 4 h incubation at 37°C ejaculated bull sperm contained less than 2 Jlmol of total nucleotides per 10 9 sperm compared to at least 10 Jlmol in incubated epididymal sperm. This difference in concentration largely arose through the destruction of most of the nucleotides measured in epididymal sperm by the nucleosidase, this effect occurring within 1 min of ejaculation.…”

Section: Discussionmentioning

confidence: 97%

“…The enzyme destroys most of the oxidized pyridine nucleotide coenzymes measured in washed epididymal sperm within 1 min of ejaculation (Bistocchi et al 1968). These coenzymes are important for the maintenance of motility and the metabolism of spermatazoa (Brookes and Mann 1971).…”

Section: Introductionmentioning

confidence: 99%

Pyridine Nucleosidase in Bull Semen I. Breed and Sire Differences in Enzyme Concentration

Kl¹,

Giles²,

Hart³

1975

Aust. Jnl. Of Bio. Sci.

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The concentration of a pyridine nucleosidase which cleaves the nicotinamide-ribose bond in NAD and related compounds was assayed using the cyanide addition reaction in semen samples collected by artificial vagina from 246 bulls. Among the 205 sires of recognized dairy breeds the nucleosidase concentration ranged from 0 to 1470 units/ml semen. Of the dairy sires 18 % produced semen containing no nucleosidase activity. Among the 41 sires of recognized beef breeds 54 % had no nucleosidase and the highest concentration was 630 units/ml semen.Among 20 sires from each of which 5-17 collections were assayed, there were significant differences in average nucleosidase concentration. There was a discontinuous distribution in nucleosidase concentration among the 169 dairy sires producing semen with measurable enzyme activity. Results for 18 dairy sires each with from 4 to 16 sons showed that sires with no seminal nucleosidase produced more sons with no enzyme or lower concentrations of enzyme than sires with higher nucleosidase concentrations. It is suggested that the concentration of the nucleosidase in bull semen is simply inherited.

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“…The concentrations of nicotinamide coenzymes expressed in nmol./10 9 sperm vary between species (Brooks & Mann 1971) and between epididymal and ejaculated sperm within species (Bistocchi et al 1968). Nicotinamide adenine dinucleotide glycohydrolase (EC 3.2.2.5) has been purified from bull semen (Yuan & Anderson 1971) and is most likely the pyridine nucleosidase that hydrolyses over 60 percent of the NAD and NAD P possessed by bovine epididymal sperm within minutes of ejaculation (Bistocchi et al 1968).…”

Section: Introductionmentioning

confidence: 99%

“…Nicotinamide adenine dinucleotide glycohydrolase (EC 3.2.2.5) has been purified from bull semen (Yuan & Anderson 1971) and is most likely the pyridine nucleosidase that hydrolyses over 60 percent of the NAD and NAD P possessed by bovine epididymal sperm within minutes of ejaculation (Bistocchi et al 1968).…”

Section: Introductionmentioning

confidence: 99%

The activity of pyridine nucleosidase in bull semen and its relationship to fertility

Hart

Giles

1975

New Zealand Journal of Agricultural Research

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The concentration of pyridine nucleosidase in single samples of semen obtained from each of 39 sires ranged from zero to 1470 units per mI. Semen from each sire was routinely processed in Caprogen containing catalase and the average conception rates 0-to 49-day percent non-return rate for first inseminations) ranged from 57.2 to 72.6 percent. The correlation coefficient between enzyme concentration and conception rate was only 0.19. Average conception rate for the 14 sires not producing seminal pyridine nucleosidase was 64.3 (S.D. ± 3.8) percent compared with 65.4 (± 3.4) percent for the remaining 25 sires. The presence or absence of an enzyme which destroys most of the nicotinamide coenzymes possessed by epididymal sperm did not adversely alter the fertility of sperm diluted in Caprogen containing catalase. Although Caprogen contains hexanoic acid, the concentration of 0.25 mg per ml was insufficient to inhibit pyridine nucleosidase activity. Nicotinamide can also inhibit enzyme activity, but the addition of 0.1 mg of nicotinamide per ml of Caprogen reduced conception rate by 1.9 percent (p < 0.01). No pyridine nucleosidase activity was detected in semen samples from eight rams.

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Pyridine-Nucleotide Coenzymes in Bull and Rabbit Spermatozoa

Cited by 16 publications

References 5 publications

Pyridine Nucleosidase in Bull Semen ll. Biochemical Properties

Pyridine Nucleosidase in Bull Semen ll. Biochemical Properties

Pyridine Nucleosidase in Bull Semen I. Breed and Sire Differences in Enzyme Concentration

The activity of pyridine nucleosidase in bull semen and its relationship to fertility

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