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  • 11
    Electronic Resource
    Electronic Resource
    Radial diffusion in gel for micro determination of enzymes
    Amsterdam : Elsevier
    Analytical Biochemistry 46 (1972), S. 502-533 
    Details
    ISSN: 0003-2697
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1016/0003-2697(72)90324-7
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  • 12
    Electronic Resource
    Electronic Resource
    Männliche Sterilitätsfaktoren (1979)
    Springer
    Archives of gynecology and obstetrics 228 (1979), S. 467-478 
    Details
    ISSN: 1432-0711
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02427517
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  • 13
    Electronic Resource
    Electronic Resource
    Bilateral tubal pregnancy following in vitro fertilization and embryo transfer (1983)
    Springer
    Archives of gynecology and obstetrics 234 (1983), S. 75-78 
    Details
    ISSN: 1432-0711
    Keywords: Bilateral tubal pregnancy ; In vitro fertilization in the case of a woman with patent fallopian tubes
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary A case of bilateral tubal pregnancy resulting from in vitro fertilization and the transfer of two embryos is reported. Because the husband had retrograde ejaculation after surgical treatment of a malignant testicular tumour, cryopreserved semen was used.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02114729
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  • 14
    Electronic Resource
    Electronic Resource
    Acrosin activity and acrosomal ultrastructure of cryopreserved human spermatozoa
    Amsterdam : Elsevier
    Cryobiology 11 (1974), S. 559 
    Details
    ISSN: 0011-2240
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Medicine
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1016/0011-2240(74)90191-6
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  • 15
    Electronic Resource
    Electronic Resource
    Occurence of the kallikrein-kinin system in human genital tract secretions and its possible function in stimulation of sperm motility and sperm migration (1976)
    Springer
    Inflammation research 6 (1976), S. 437-438 
    Details
    ISSN: 1420-908X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01973244
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  • 16
    Electronic Resource
    Electronic Resource
    Acid extraction of acrosin from human spermatozoa pretreated by different physicochemical methods (1982)
    Springer
    Archives of dermatological research 273 (1982), S. 273-285 
    Details
    ISSN: 1432-069X
    Keywords: Acrosin ; Acrosome ; Acid extraction ; Snap freezing ; Physicochemical methods ; Zymogen activation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Washed human spermatozoa were subjected to different physicochemical methods, followed by acid extraction of the sperm acrosomes to dissolve acrosin. The acrosin activity of the sperm pellet and the supernatant was determined by benzoyl arginine ethyl ester/alcohol dehydrogenase (BAEE/ADH) assay to calculate the total acrosin activity in m U/106 spermatozoa. Membrane-active and zymogen-activating agents increased the total acrosin activity 50%–200% compared to acid extraction alone. Similar results were obtained by osmotic shock, sonication and treatment with glass beads. Snap freezing of unprotected spermatozoa in liquid nitrogen yielded a fivefold increase in total acrosin activity, thus demonstrating that this is the method of choice for optimal acrosin extraction. The possibility is discussed as to whether acrosomal membrane alterations with improved solubilization of membranebound acrosin and/or conformational changes and/or zymogen activation are responsible for the considerable increase observed in acrosin activity.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00409256
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  • 17
    Electronic Resource
    Electronic Resource
    Determination of active, non-zymogen acrosin, proacrosin and total acrosin in different andrological patients (1990)
    Springer
    Archives of dermatological research 282 (1990), S. 335-342 
    Details
    ISSN: 1432-069X
    Keywords: Acrosin active, non-zymogen ; Proacrosin ; Acrosomal membrane stability/disturbances ; Fertility/sterility
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary A spectrophotometric assay is described which, due to improved extraction conditions, allows quantitative determination of enzymatically active, non-zymogen acrosin, proacrosin and total acrosin activity from human sperm acrosomes. Acrosomal proteinase activity is assessed by acid extraction of the sperm pellet and the suspension medium before and after snap-freezing, followed by zymogen autoactivation. Release of acrosin from the acrosome can be used as a sensitive biochemical marker to characterize acrosomal membrane stability, severe disturbance of which may be the cause of impaired male fertility. Acrosin activities in different populations of semen specimens are reported and compared to data available in the literature. Different degrees of acrosomal membrane alterations are observed in men with oligozoospermia, teratozoospermia and polyzoospermia. Particularly in oligozoospermia, a significant increase of active, nonzymogen acrosin points to severe acrosomal membrane alterations and, in addition, to a premature activation of proacrosin, which may impair fertilization in certain individuals. Finally, acrosin activity is shown to be significantly influenced by the time of sexual abstinence. It is concluded that determination of acrosin may be a useful indicator of the fertility potential in men.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00375729
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  • 18
    Electronic Resource
    Electronic Resource
    Electron microscopic localization of a fucose-binding protein in acrosome reacted boar spermatozoa by the fucosyl-peroxydase-gold method (1987)
    Springer
    Histochemistry and cell biology 86 (1987), S. 297-303 
    Details
    ISSN: 1432-119X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary In this study we have examined the behaviour and the localization of the fucose-binding protein (FBP) in boar spermatozoa during ionophore induced acrosome reaction (AR) by means of normal TEM and specimen preparation in toto. During early stages of AR the FBP is first localized at the border between equatorial segment and anterior acrosome. With the propagation of the AR the FBP is dramatically expressed and visible over the entire surface of the acrosome and equatorial segment. TEM pictures of this stages show that the FBP is associated with the OAM. At later stages of AR, when acrosomal ghost formation occur, the FBP is associated with the acrosomal ghost, and equatorial segment and to a very low degree also with the IAM. It is concluded from this data that the FBP is responsible for the specific binding of the ghost-sperm unit to the zone pellucida.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00490262
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  • 19
    Electronic Resource
    Electronic Resource
    Boar sperm membranes antigens (1990)
    Springer
    Histochemistry and cell biology 93 (1990), S. 491-495 
    Details
    ISSN: 1432-119X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary The dynamics of the cell surface during the process of capacitation is impressively shown by means of a monoclonal antibody directed against the P86/5 antigen. This glycoprotein was located in the sperm plasma membrane using the colloidal gold method in combination with specimen preparation in toto. The antigen is absent at the rostral tip of non-capacitated spermatozoa, but forms clusters over the principal segment and the equatorial segment after induction of capacitation. This formation of microdomains with different properties may be a prerequisite for the onset of the acrosome reaction (AR). During AR the diffusion barrier for the P86/5 antigen breakes down and the antigen occupies now the rostral crescent-like area of the sperm head. These observations are discussed with respect to zona binding and induction of the AR in boar spermatozoa.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00266406
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  • 20
    Electronic Resource
    Electronic Resource
    Boar sperm membranes antigens (1990)
    Springer
    Histochemistry and cell biology 93 (1990), S. 485-490 
    Details
    ISSN: 1432-119X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary A monoclonal antibody, designated mAb P86/5, was generated by immunization of female Balb/c mice with a membrane vesicle fraction composed of the outer acrosomal membrane and plasma membrane (PM-OAM). As determined by fluorescence microscopy and electron microscopy P86/5 recognizes a sperm plasma membrane antigen that is restricted to the sperm head. In intact spermatozoa the P86/5-antigen is distributed over the surface of the sperm head with the exception of the rostral region. By comparing the antibody binding pattern generated at 4° C and 25° C, it could be shown that the P86/5-antigen is capable to diffuse freely within the cell membrane overlying the acrosome whereas its lateral mobility is restricted to the post-acrosomal region. The P86/5-antigen had a molecular weight of about 78 kDa as revealed by SDS-PAGE and western blotting. The glycoprotein nature of the P86/5-antigen was established by lectin affinity chromatography.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00266405
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