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  • 1
    Electronic Resource
    Electronic Resource
    Physical properties and function of phallolysin (1983)
    s.l. : American Chemical Society
    Biochemistry 22 (1983), S. 4574-4580 
    Details
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/bi00288a035
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  • 2
    Electronic Resource
    Electronic Resource
    An On-Line System for Storage and Retrieval of Polymer Data (1979)
    s.l. : American Chemical Society
    Journal of chemical information and modeling 19 (1979), S. 73-76 
    Details
    ISSN: 1520-5142
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/ci60018a006
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  • 3
    Electronic Resource
    Electronic Resource
    Photoaffinity labelling of nuclear steroid 5α-reductase of rat ventral prostate
    Amsterdam : Elsevier
    Journal of Steroid Biochemistry 33 (1989), S. 379-387 
    Details
    ISSN: 0022-4731
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://linkinghub.elsevier.com/retrieve/pii/0022-4731(89)90327-0
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  • 4
    Electronic Resource
    Electronic Resource
    Purification and characterization of transglutaminases from the genital tract of the male rat
    Amsterdam : Elsevier
    Journal of Chromatography A 587 (1991), S. 55-60 
    Details
    ISSN: 0021-9673
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://linkinghub.elsevier.com/retrieve/pii/0021-9673(91)85197-N
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  • 5
    Electronic Resource
    Electronic Resource
    Immunocytochemical localization of actin and tubulin in rat testis and spermatozoa (1988)
    Springer
    Histochemistry and cell biology 89 (1988), S. 261-267 
    Details
    ISSN: 1432-119X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Using commercial monoclonal antibodies against actin and tubulin (α and β), the respective antigens were localized on semithin and ultrathin sections of the rat testis. Tubulin immunofluorescence was found in the socalled manchette surrounding the heads of the maturating spermatids as well as the sperm tail. The distribution pattern varied with sperm development. Modified Sertoli cells found at the transition between the seminiferous tubules and the rete testis displayed much filamentous tubulin-reactive material. The immunofluorescence findings could be confirmed at the ultrastructural level using the indirect immunogold method. Actin immunofluorescence was demonstrated in vascular smooth muscle cells, interstitial macrophages and — most intensely — in peritubular cells. Inside the seminiferous tubules the Sertoli cell junctions and the ectoplasmic specializations of the Sertoli cells that follow the outer contour of spermatid heads displayed distinct actin immunofluorescence. In addition to the locations mentioned, actin-like immunoreactivity was visualized at the ultrastructural level in the chromatoid body and the subacrosomal space of spermatids as well as on the outer dense fibers of the sperm tail. Immunoblotting experiments with actin antibodies showed that in extracts from testicular spermatozoa, intact or fragmented into heads and tails, from isolated Sertoli cells grown in vitro, and from testis tissue in addition to authentic actin a protein was present in sperm tail extracts that strongly bound the actin antibody. This protein may be an actin-related protein and may be responsible for the actin-like immunoreactivity of the outer dense fibers of the sperm tail.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00493150
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  • 6
    Electronic Resource
    Electronic Resource
    Cytochemistry and biochemistry of acid phosphatases (1980)
    Springer
    Histochemistry and cell biology 67 (1980), S. 99-111 
    Details
    ISSN: 1432-119X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Acid phosphatases of the rat ventral prostate were studied cytochemically using different substrates. The results were compared to findings on isoelectric focussing gels stained for acid phosphatase activity. This is a highly specific and reproducible method which allows the distinction between secretory androgen-dependent and lysosomal acid phosphatases. Activity of lysosomal acid phosphatase was increased after castration, while the activity of the secretory enzyme gradually decreased after androgen deprivation. None of the substrates tested was selectively hydrolyzed by either secretory or lysosomal acid phosphatase. Phenylphosphate, creatine phosphate and choline phosphate were found to be inappropriate substrates for histochemical purposes, however, reproducible results were obtained with α-naphthylphosphate, β-glycerophosphate and p-nitrophenylphosphate. The method of isoelectric focussing (pH range 4.0–8.0) of enzymes with subsequent histochemical staining demonstrated lysosomal enzymes at pH 7.9 and 8.2 respectively. Small amounts of identical enzymes were found in liver, kidney, blood or epididymis. Secretory acid phosphatases were focussed at pH 5.5, 5.6, 5.65 and 7.15. Similar enzymes have been identified in epididymis, kidney, liver and pancreas. These results indicate that 1) at present no “specific” substrate for prostatic secretory or lysosomal acid phosphatases is available and 2) that no prostate-specific “prostatic acid phosphatase (PAP)” exists in the rat ventral prostate.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00490092
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  • 7
    Electronic Resource
    Electronic Resource
    Intracellular localization of prostatic binding protein (PBP) in rat prostate by light and electron microscopic immunocytochemistry (1982)
    Springer
    Histochemistry and cell biology 76 (1982), S. 497-516 
    Details
    ISSN: 1432-119X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Extra- and intracellular distribution of Prostatic Binding Protein (PBP) was studied in the different genital organs of the male rat by immunocytochemistry at the light and electron microscopic levels. PBP was extracted from cytosols of rat ventral prostate and used for immunization of rabbits. The specificity of the antiserum raised was tested by “western blotting” and immunoelectrophoresis. From the different fixatives tested for optimal structural and antigenic preservation of the ventral prostate a mixture containing 2.5% paraformaldehyde, 0.5% glutaraldehyde and 0.5% CaCl2 in cacodylate buffer, 0.05 M, pH 7.3 was selected. Using the immunofluorescence technique and the unlabeled antibody enzyme method PBP-immunoreactivity was detected at the light microscopic level in the luminal secretions of the ventral prostate. No reaction was observed with the seminal vesicle, the coagulating gland, the dorsal and lateral prostates, the epididymis and the testis. Intracellular secretory granules reacting with PBP antiserum were exclusively found in the secretory cells of the ventral prostate. Insufficiently fixed cells showed a diffuse generalized reaction of the cytoplasm indicating a leakage of the antigen from the secretory granules. Such artifacts were common in tissue sections processed with the preembedding-staining procedure. At the ultrastructural level therefore mostly the postembedding staining method was performed using both the unlabeled antibody enzyme method and the ferritin-labeled immunoglobulin technique in osmicated, Epon-embedded tissue. Labeling with either method was intense in the secretory granules and the condensing vacuoles, while the labeling density of the rough endoplasmic reticulum and the Golgi cisternae was in the background range. Castration experiments showed that secretory material displaying PBP immunoreactivity was retained within the acinar lumen of the gland for several days after castration, but was absent from most secretory cells already by four days after castration. Immunocytochemistry of PBP therefore is a very sensitive method for analysing the secretory activity and its androgen dependence of the prostate of the rat.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00489905
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  • 8
    Electronic Resource
    Electronic Resource
    Ultrastructural localization of uteroglobin immunoreactivity in rabbit lung and endometrium, and rat ventral prostate (1985)
    Springer
    Histochemistry and cell biology 83 (1985), S. 413-417 
    Details
    ISSN: 1432-119X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Recent biochemical studies have demonstrated amino acid sequence homologies between uteroglobin from rabbit endometrium and prostatic binding protein from rat ventral prostate. We have studied the ultrastructural distribution of uteroglobin-immunoreactive material in rabbit lung and endometrium and rat ventral prostate using an uteroglobin antibody raised in guinea pigs. Secretory granules of bronchiolar Clara cells, endometrial non-ciliated cells and rat prostate secretory cells gave a positive immunoreaction when this antibody was used. The results indicate a close relationship of immunoreactive epitopes of proteins present in those secretory cells. The functional properties of these proteins (glycoproteins, steroid binding, androgen-dependent secretion) suggest a close functional relationship, for instance a surface action such as coating, capping, masking or lubrication.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00509202
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  • 9
    Electronic Resource
    Electronic Resource
    Immunohistochemistry of secretory transglutaminase from rodent prostate (1990)
    Springer
    Histochemistry and cell biology 93 (1990), S. 525-530 
    Details
    ISSN: 1432-119X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Transglutaminases are Ca2+-dependent intra-and extracellular enzymes catalyzing the cross-linking between proteins and/or polyamines, thereby eliciting divergent physiological effects such as fibrin clot stabilization or hair follicle cross-linking. A secretory transglutaminase (EC 2.3.2.13) was isolated from the coagulating gland of the rat. The protein is highly glycosylated. A fraction purified to homogeneity was used as an antigen to raise polyclonal antibodies in rabbits. These antibodies were used to identify the secretion sites of the protein within the male accessory sex glands as well as to study the immunological relationships of the respective antigen within different organs of different species. In the rat, the coagulating gland and likewise the dorsal prostate gave a positive immunoreaction. In the guinea pig, a closely related protein was detected in the anterior prostate. No cross-reactivity was found with membrane-bound transglutaminase from liver, erythrocytes or blood clotting factor XIIIa. The intraluminal secretion of the aforementioned glands was only weakly stained. No secretory granules were observed in the glandular epithelium but instead bleb-like structures reminiscent of apocrine secretion. A slight background stain of the epithelium remained even in castrated animals where secretion is largely suppressed. The background stain is attributed to a tissue-type, membrane-bound, non-secretory transglutaminase that is not androgen dependent, but instead synthesized only after androgen deprivation.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00266412
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  • 10
    Electronic Resource
    Electronic Resource
    Stage-dependent appearance of sulfhydryl oxidase during spermatogenesis in the testis of rat and hamster (1990)
    Springer
    Histochemistry and cell biology 94 (1990), S. 365-371 
    Details
    ISSN: 1432-119X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Sulfhydryl oxidase (SOx), an enzyme that catalyzes the oxidation of sulfhydryl compounds, appears in the spermatogenic cells of rat and hamster testes in a stage-dependent manner. It first appears in pachytene spermatocytes at stage I in both the animal species studied. SOx immunoreactivity is associated with mitochondria of these cells. The fate of such mitochondria is species-dependent. In rat, the immunoreactive mitochondria aggregate during maturation phase and are retained in the residual bodies. Spermatozoa free of SOx are released into the lumen. On the other hand, in hamster, the immunoreactive mitochondria arrange themselves around the midpiece of spermatozoa. In such a case, residual bodies lack SOx. The appearance of SOx coincides with the appearance of LDH-X in the spermatogenic cells. Like many other proteins such as LDH-X, RSA-1 and cytochrome ct, SOx provides yet another example of differential gene activation associated with a developmental process of gametes.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00266442
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