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  • 1
    Electronic Resource
    Electronic Resource
    New York, NY : Wiley-Blackwell
    Gamete Research 2 (1979), S. 35-42 
    ISSN: 0148-7280
    Keywords: activated motility ; temperature dependence of motility ; sperm transport ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The motility of rabbit spermatozoa recovered from the vagina, endocervix, uterus, and four regions of the oviduct was assessed visually by phase-contrast microscopy at intervals from one minute to 16 hours after a single mating. The percentage of motile cells in each sample was dependent on the temperature of recovery, ie, 23° vs 37°C, but was not influenced by the temperature of observation. Spermatozoa in the lower isthmus of the oviduct were the most temperature sensitive population to recovery at 23°C. When all manipulations and observations were performed at 37°C, the percentage of spermatozoa with progressive motility varied according to the region sampled and interval after mating. Populations from the vagina, uterus and upper regions of the oviduct usually had a high proportion of progressively motile cells with vigorous flagellar activity. Fewer spermatozoa showed progressive movement on recovery from the endocervix and lower 2 cm of the tubal isthmus and their flagellar activity was generally depressed. The decrease in flagellar beat frequency noted in the latter regions may be a major factor limiting sperm ascent in the female tract. A unique pattern of “activated” motility was seen exclusively in populations taken from the oviducts at 6 to 16 hours after mating. This motility pattern, consisting of alternating episodes of linear progressive and vigorous nonprogressive movement, may be analogous to the activated motility described for capacitated rodent spermatozoa.
    Additional Material: 1 Ill.
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  • 2
    Electronic Resource
    Electronic Resource
    New York, NY : Wiley-Blackwell
    Gamete Research 7 (1983), S. 277-288 
    ISSN: 0148-7280
    Keywords: sperm head/tail junction ; aldimine bonds ; sperm head detachment ; head/tail stabilization ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Rabbit spermatozoa recovered from the reproductive tract of females 12-13 hr postcoitum resisted head/tail separation induced by n-butylamine and dithiothreitol, but not sodium dodecylsulfate. Stabilization of the sperm head/tail junction also developed in vitro at 37°C in physiological media and in saline-Tris-HCl (pH 7.4). Resistance to dithiothreitol occurred in motile, but not immotile spermatozoa. Only nonmotile spermatozoa developed resistance to sodium dodecylsulfate in vitro, whereas both motile and immotile spermatozoa became resistant to n-butylamine. Stabilization to n-butylamine was time and temperature dependent and was accelerated by Cu2+, Mg2+, and Zn2+, but not Mn2+. The resistance of hamster and rabbit spermatozoa to n-butylamine developed in physiological media over the same time intervals as required for capacitation and the acquisition of hyperactivated motility.Reagents that react with sulfhydryl groups had no effect on the development of resistance to n-butylamine but inhibited stabilization to sodium dodecylsulfate, suggesting that the latter stabilization may result from the formation of disulfide crosslinks at the head/tail junction. Reduction of aldehyde groups by sodium cyanoborohydride did not prevent stabilization to sodium dodecylsulfate, but did reduce detachment by dithiothreitol. Aldehyde groups thus are not involved in the stabilization of the head/tail junction to sodium dodecylsulfate, but may participate in new crosslinks stabilizing the head/tail junction to dithiothreitol. Inhibitors of transglutaminase did not prevent development of resistance to n-butylamine, sodium dodecylsulfate, or dithiothreitol indicating that head/tail stabilization does not involve intermolecular γ-glutamyl-∊-dysine bonds.
    Additional Material: 6 Tab.
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  • 3
    Electronic Resource
    Electronic Resource
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 32 (1986), S. 207-214 
    ISSN: 0730-2312
    Keywords: monoclonal antibody DWP ; activated ras protein reactive antibody ; anti-ras antibodies ; anti-ras monoclonal antibody ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Activated ras transforming genes have been described in a variety of neoplasms and encode 21,000-Dalton (p21) proteins with amino acid substitutions at positions 12, 13, and 61. In this report we describe a monoclonal antibody designated DWP that reacts. Specifically with synthetic dodecapeptides containing valine at position 12, to a lesser extent with peptides containing cysteine at position 12 and not with peptides containing glycine, arginine, serine, aspartic acid, glutamic acid or alanine at the same position. Western blot and immunoperoxidase studies showed that DWP specifically reacts with activated rasH or rasK proteins in NIH cells transformed by DNA from the human carcinoma cells that encode valine at position 12. DWP did not react with normal p21s encoding glycine at position 12, nor with activated p21s encoding aspartic acid, glutamic acid, arginine, serine, or cysteine at position 12. A survey of human tumor cell lines demonstrated that DWP reacted with the human bladder carcinoma cell line T24 but not with human tumor cell lines previously shown td contain other activating mutations at positions 12 or 61. DWP and perhaps additional antibodies that specifically react with alterations at positions 12 or 61 of the ras protein may be valuable in determining the presence and frequency of activated ras proteins in human malignancy.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
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