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SCANNING ELECTRON MICROSCOPY OF THE HUMAN, GUINEA-PIG AND RHESUS MONKEY SEMINAL COAGULUM

L. J. D. ZANEVELD, P. F. TAUBER, C. PORT, D. PROPPING, and G. F. B. SCHUMACHER

Summary.

A relationship appears to exist between the morphological appearance of the seminal coagulum and the rate of its liquefaction. The guinea-pig and rhesus monkey coagula liquefy only poorly, and consist of thick fibres which form a solid structure. A normal human coagulum possesses an extensively organized network of long thin fibrous strands. A `slow liquefying' human ejaculate shows similar patterns although it possesses a multitude of thick fibres. As the coagulum liquefies, the fibres become disorganized and turn into spherical material. Spaces within the fibrous network of the human coagulum are so small that escape of spermatozoa does not seem possible without liquefaction. This may explain the subfertility of poorly liquefying or non-liquefying human semen.

DOI:
https://doi.org/10.1530/jrf.0.0400223
Volume 40: Issue 1,
Pages:
223–225 (3 total)
Free access

Components of human split ejaculates

P. F. Tauber, L. J. D. Zaneveld, D. Propping, and G. F. B. Schumacher

Summary.

Lysozyme, α-amylase, neutral proteinase and plasminogen activator were most concentrated in the initial portion of the ejaculate that consists mostly of Cowper's gland and prostate gland fluids as well as spermatozoa. The concentration of the high molecular weight proteinase inhibitors, α1-antitrypsin and α1x-antichymotrypsin, was essentially unaltered throughout the ejaculate fractions, although their absolute amounts showed an increase towards the final fraction. By contrast, the total inhibitory activity towards pancreatic trypsin was highest both in concentration and amount in the last fraction, thus indicating that the seminal vesicles are its primary source. Plasminogen, prothrombin, Factor XIII, and the proteinase inhibitors antithrombin III, α2-macroglobulin, inter-α-trypsin inhibitor and C1s-inactivator could not be detected immunochemically in whole ejaculates, and indicates the dissimilarity between the coagulation/liquefaction processes of semen and blood.

DOI:
https://doi.org/10.1530/jrf.0.0460165
Volume 46: Issue 1,
Pages:
165–171 (7 total)
Free access

COMPONENTS OF HUMAN SPLIT EJACULATES

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.

DOI:
https://doi.org/10.1530/jrf.0.0430249
Volume 43: Issue 2,
Pages:
249–267 (19 total)