Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0272170 (SDS)
 50,377 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The epididymis of the ram synthesizes under androgenic control of specific 64 kD protein. The purified protein appeared as a single band in SDS polyacrylamide gel electrophoresis. It was labelled and an antiserum was prepared in mice. Results showed localization of receptors sites for 64 kD on the periacrosomal plasma membrane of testicular spermatozoa. The protein itself was found on the periacrosomal area of both epididymal and ejaculated spermatozoa.
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PMID:[Localization, on the head of ram spermatozoa, of affinity sites for the 64kD androgen dependent epididymal prealbumin]. 313 11

The major fucose-binding protein of 53 kDa was isolated from boar spermatozoa by mild detergent extraction and subsequent high-performance gel filtration and reversed-phase high-performance liquid chromatography. This protein has been identified as high-molecular-mass acrosin by N-terminal sequencing. Treatment of the isolated protein with diisopropyl fluorophosphate abolishes the enzymatic activity but not the zona pellucida- and fucose-binding properties. Mercaptolysis and S-pyridyl-ethylation of native two-chain acrosin followed by HPLC and SDS-PAGE revealed that the binding properties are located on the acrosin heavy chain.
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PMID:Zona pellucida-binding and fucose-binding of boar sperm acrosin is not correlated with proteolytic activity. 316 67

The acrosome reaction of spermatozoa from the starfish Marthasterias glacialis was induced with the ionophore A23187. Reacted cells were then processed for acid phosphatase ultrastructural cytochemistry, but significant enzyme activity was not detected. However, when the supernates from suspensions of ionophore-treated sperm were assayed for acid phosphatase, a net enzyme activity was observed. Supernatant proteins were run in starch gel electrophoresis and fluorescent zymograms revealed a single band of acid phosphatase. SDS-PAGE of proteins eluted from the active spots of starch gels showed one major band of about 63 kDa. The results obtained support the hypothesis that the acid phosphatase whose activity has been detected only at the time of binding of sperm and egg originates from the sperm acrosome.
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PMID:Starfish acrosomal acid phosphatase: a cytochemical and biochemical study. 319 Dec 93

The selection of motile human spermatozoa, from fertile and infertile semen samples was compared by using Percoll density gradient centrifugation or the swim-up procedure. Selected spermatozoa were evaluated according to their motility, % normal forms, nuclear maturity (aniline blue staining, acridine orange staining, ethidium bromide uptake and SDS nuclear decondensation). These methods showed differences between fertile and infertile men. The swim-up procedure, based on motility, resulted in greater proportions of motile spermatozoa and eliminated mainly tail abnormalities. Percoll gradient separation, based on density, selected oval-headed spermatozoa with good motility. Nuclear maturity level was improved by both methods but Percoll gradient separation generally resulted in spermatozoa with better nuclear maturity than those selected by the swim-up procedure.
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PMID:Nuclear maturity and morphology of human spermatozoa selected by Percoll density gradient centrifugation or swim-up procedure. 319 73

We report in this paper that proteins from the surface of ejaculated spermatozoa contain antigenic determinants cross-reacting with a rabbit antiserum raised against native CFS, a protein secreted from the rat seminal vesicle and composed of two subunits, namely RSV IV and RSV V. Conversely, no such proteins could be extracted from cauda epididymal spermatozoa. The cross-reacting proteins derived from the ejaculated spermatozoa were analyzed by SDS-PAGE. An electrophoretic pattern different than that expected for native CFS in denaturing conditions was found. In vitro reconstitution experiments showed that labeled native CFS is able to bind cauda epididymal spermatozoa. The CFS protein recovered from the sperm surface was examined and alterations of its structure were also noted. The sperm-coating abilities of CFS and of its RSV IV subunit are discussed.
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PMID:Detection of sperm-coating antigens immunologically related to a seminal protein in rat. 324 84

Vasectomy was performed on inbred Lewis rats to induce anti-sperm autoantibodies and to identify their cognate autoantigens. Different detergent extracts of cauda epididymal spermatozoa were separated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), blotted to nitrocellulose, and probed with sera from pre-vasectomy, post-vasectomy, and hyperimmunized animals to detect isologous sperm antigens. Nonreduced SDS-soluble autoantigens at greater than 200, 86, 43, and 26 kDa were bound by post-vasectomy antisera. Reduction of SDS-soluble antigens resulted in increased staining of the 86, 72-63, and 43 kDa autoantigens. Laemmli extraction of SDS insoluble pellets with beta-mercaptoethanol generated the largest repertoire of autoantigens including several autoantigens found in SDS-soluble extracts. Therefore, to analyze the entire repertoire of post-vasectomy autoantigens, whole sperm were extracted with Laemmli buffer under reducing conditions. Autoantiserum from most vasectomized animals bound Laemmli-extracted reduced autoantigens of approximately 86 (89-78), 63, 43, and 20 (21-16) kDa. Testicular extracts, reduced and separated by SDS-PAGE, contained autoantigens of 76, 60, and 42 kDa that were also recognized by hyperimmune and post-vasectomy antisera. The repertoire of sperm antigens recognized by pooled serum from hyperimmunized animals was similar to the cumulative repertoire recognized by post-vasectomy sera. These studies define several major sperm autoimmunogens recognized by post-vasectomy antisera and indicate that many of these peptide autoimmunogens are disulfide-bonded complexes.
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PMID:Post-vasectomy sperm autoimmunogens in the Lewis rat. 326 39

The acrosomal matrix of hamster spermatozoa was enriched and characterized. Acrosomal matrices were released from spermatozoa with shaking in a pH 5.2 buffer containing Triton X-100 and protease inhibitors, and enriched on a glass-bead column. Phase-contrast microscopy indicated that 70-80% of the acrosomal matrices were released from the spermatozoa and only minor contamination from sperm heads was detected. Transmission electron microscopy confirmed the low level of contamination in the preparation and revealed a bilaminar structure similar but not identical to that of guinea-pig acrosomal matrix. One- and two-dimensional SDS-polyacrylamide gel electrophoresis (SDS-PAGE) showed the acrosomal matrix to be a complex structure enriched for several polypeptides. Proteinase activity was demonstrated by gelatin-SDS-PAGE. The major activity corresponded to bands of relative molecular masses (Mr) of 56,000, 51,000 and 48,000 with two minor bands of Mr 30,000 and 28,000. The lectin Pisum sativum agglutinin (PSA) bound to the anterior head of spermatozoa and isolated acrosomal matrix as judged by fluorescence microscopy using FITC-PSA. Western blots of spermatozoa and acrosomal matrices followed by overlay with biotinylated PSA indicated that there are at least two PSA-binding glycoproteins of Mr 60,000 and 72,000.
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PMID:Characterization of isolated acrosomal matrices from hamster spermatozoa. 329 98

Previously, we demonstrated that surface radiolabeling of rat epididymal spermatozoa by lactoperoxidase-catalyzed iodination reveals a major component with an apparent molecular weight of 26,000 to 28,000 daltons (26 kDa) on spermatozoa from the cauda but not the caput epididymidis. To characterize this surface component further, sperm surface constituents radiolabeled by lactoperoxidase-catalyzed iodination were separated by 2-D PAGE. The 26 kDa component was localized by autoradiography and appeared as the major labeled acidic spot on cauda spermatozoa, but neither a radiolabeled spot nor a corresponding stained spot was present on caput spermatozoa. The 26 kDa spot was excised from 2-D gels of plasma membranes from cauda spermatozoa and utilized for immunization. The monospecific antiserum stained a single band of 26 kDa on Western blots of SDS-PAGE-separated plasma membranes from cauda spermatozoa and in a 100,000 X g supernatant fluid of the luminal contents of the cauda epididymidis. Immunohistochemical staining of cauda spermatozoa revealed antigen exclusively on the flagellar domain; the antigen was not seen on caput spermatozoa but first appeared in spermatozoa from the proximal corpus epididymidis. Immunoelectron microscopy confirmed the 26 kDa component was localized to the external face of the flagellar plasma membrane. Immunohistochemical staining of caput spermatozoa incubated in vitro with cauda epididymal luminal fluid revealed the 26 kDa component specifically bound the flagellar domain of immature spermatozoa.
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PMID:Modification of the rat sperm flagellar plasma membrane during maturation in the epididymis. 330 69

A murine monoclonal antibody raised against hamster spermatozoa was found to cross-react with human spermatozoa. By immunofluorescence, the antigen was visualized over the equatorial segment of human sperm heads. In the presence of antibody, sperm binding to the zona pellucida of salt-stored human oocytes was significantly inhibited (P less than or equal to 0.005) compared with other antibodies or control preparations. Using SDS-PAGE of whole spermatozoa and membrane preparations followed by Western blot analysis, the antigen was identified as a determinant with a relative molecular weight of 95,000.
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PMID:Monoclonal antibody against a sperm antigen Mr 95,000 inhibits attachment of human spermatozoa to the zona pellucida. 330 84

Actin was identified in boar and mole spermatozoa by utilizing indirect immunofluorescence, immunoelectron microscopy, and SDS-PAGE, followed by blot and screening with an anti-actin monoclonal antibody. Actin was detected in two places in the sperm head: the equatorial segment of the acrosome and the postacrosomal region. The protein was present in a nonfilamentous form and was localized under the plasma membrane. A small amount of actin was also detected in the sperm tail. The function of actin in the sperm head is discussed.
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PMID:Localization and distribution of actin in mammalian sperm heads. 331 22


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