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  • Author: L. J. D. Zaneveld x
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P. F. TAUBER, L. J. D. ZANEVELD, D. PROPPING and G. F. B. SCHUMACHER

Summary.

The concentrations of spermatozoa, fructose, IgG, IgA, albumin, lactoferrin, transferrin, secretory piece of IgA, β1C/β1A-globulin (C′3-component of complement), ceruloplasmin and fibrinogen were evaluated in human split ejaculates and/or in whole human seminal plasma. The concentrations of spermatozoa, IgG, IgA, albumin and transferrin decreased from the first portion of the split ejaculate to the last, indicating that these proteins originate mostly from secretions other than the seminal vesicles. By contrast, the highest amounts of fructose and lactoferrin were present in the final portion of the split ejaculates, showing their seminal vesicle origin. No secretory piece, IgM, β1C/β1A-globulin, ceruloplasmin or fibrinogen could be detected in human semen. An unidentified antigen was found that has a relatively high molecular weight and shows β1-mobility on immunoelectrophoresis.

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A. K. Bhattacharyya, L. J. D. Zaneveld, B. M. Dragoje, G. F. B. Schumacher and J. Travis

Summary.

Twenty-two synthetic proteinase inhibitors were tested for their inhibitory properties towards human acrosin. p-Nitrophenyl-p1-guanidino benzoate (NPGB) was the most effective (K1 value of 1·5 × 10−8 M), producing a non-competitive type of inhibition in contrast to all other inhibitors which showed a competitive type of inhibition. The Michaelis constant for human acrosin on BAEE at pH 8·1 was calculated to be 4·25 × 10−5 M.

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Jessie C. Goodpasture, P. M. Zavos, M. R. Cohen and L. J. D. Zaneveld

Summary. Stability of the human sperm acrosin system (major components: non-zymogen acrosin, proacrosin and acrosin inhibitor) was studied under various conditions of semen storage used clinically or in the laboratory. Freezing at −196°C caused a profound decrease in total acrosin content and in the amount of this enzyme present in zymogen form (proacrosin), but resulted in some increase in non-zymogen acrosin. Acrosin inhibitor did not appear to be significantly affected by this treatment. No relationship was present between the decreases in sperm motility induced by freezing to −196°C and the alterations in total acrosin, proacrosin and non-zymogen acrosin.

Storage of whole semen at −20°C had deleterious effects on all the components of the acrosin system measured except for non-zymogen acrosin. Major decreases in the total acrosin, proacrosin and acrosin inhibitor occurred after only 1 day at −20°C and continued slowly thereafter. Whole semen kept at room temperature for up to 24 h after ejaculation did not show any significant changes in the sperm acrosin system. Seminal plasma did not have a detrimental or stabilizing effect on acrosi[ill] and proacrosin when spermatozoa were kept at room temperature. However, removal of seminal plasma and re-suspension of spermatozoa in 0·9% NaCl resulted in the liberation of a significant amount of the acrosin inhibitor from the spermatozoa and the apparent activation of some of the proacrosin to acrosin.

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L. J. D. ZANEVELD, G. F. B. SCHUMACHER, H. FRITZ, E. FINK and E. JAUMANN

Summary.

Human sperm acrosomal proteinase is immediately inhibited by the Fraction I (mol. wt. 12,700) and Fraction II (mol. wt. 5,400) proteinase inhibitors of human seminal plasma. The Fraction II inhibitor inhibits acrosomal proteinase much more effectively than the Fraction I inhibitor, having an association constant of 5·0 × 108 m −1 and a dissociation constant of 2 ·0 × 10 − 9 m. The results provide further evidence for the possible rôle of the Fraction II inhibitor in the reproductive process.

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R. A. Anderson Jr, C. Oswald, B. R. Willis and L. J. D. Zaneveld

Summary. Ejaculates were obtained from C57BL mice by applying two successive series of electrical stimuli which were delivered via a bipolar rectal probe. The ejaculates thus collected contained fertile spermatozoa as indicated by results from in-vitro fertilization. Once separated from the seminal plasma, ejaculated spermatozoa possessed the same in-vitro fertilization rate as epididymal sperm. Ejaculates were analysed for coagulum weight, ejaculate volume, sperm count, sperm motility, acid phosphatase content and fructose content. Significant differences were present between several of these values for fertile and infertile mice, and values were therefore empirically assigned to represent minimal amounts for 'normal' fertility (1·5 μl ejaculate volume; 10·2 mg coagulum weight; 2·5 × 106 spermatozoa/ml; 2·3 × 103 motile spermatozoa/ejaculate). One half of the fertile animals had no deficiencies in any of the characteristics measured, whereas 97% of the infertile animals had at least one deficiency. No fertile male had more than 2 deficiencies. These data show that the characteristics of mouse semen obtained by the present method of electroejaculation are related to the fertility status of the animal.

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R. S. Jeyendran, H. H. Van der Ven, M. Perez-Pelaez, B. G. Crabo and L. J. D. Zaneveld

Summary. The objective of this study was to develop a relatively simple test to evaluate the functional integrity of the membranes of human spermatozoa. As in some other species, human spermatozoa 'swell' under hypo-osmotic conditions due to the influx of water and the expansion of the membranes. A mixture of equal parts of fructose and sodium citrate (150 mosmol) with calculated ionic strength of 0·15 resulted in a maximal number of clearly identifiable swollen spermatozoa. Only small variations were seen when different aliquants of the same semen samples were separately evaluated. A high correlation (r = 0·94) was obtained between expected and observed values of swollen spermatozoa when known amounts of heat-treated spermatozoa, unable to undergo swelling, were added to untreated spermatozoa. A good correlation (r = 0·90) was also observed between the % spermatozoa in a semen sample that were capable of undergoing swelling and the % of denuded hamster oocytes that were penetrated by capacitated spermatozoa from the same semen sample. By contrast, the correlations between % sperm swelling in ejaculates and % normal sperm forms, % motile spermatozoa and % spermatozoa that do not stain with eosin-Y (supravital stain) in the same ejaculates were 0·30,0·61 and 0·52, respectively. Therefore, the hypo-osmotic swelling technique to evaluate the functional integrity of the sperm membrane appears to give high repeatability and accuracy and is closely correlated to the in-vitro fertilizing ability of spermatozoa. It may be a useful addition to the standard semen analysis.