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  • 1
    Electronic Resource
    Electronic Resource
    [s.l.] : Nature Publishing Group
    Nature 214 (1967), S. 1336-1338 
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] We have recently found that both eggs and spermatozoa of sea urchins contain two kinds of glycolipids in considerable amounts5. These glycolipids seem to be neither constituents of jelly coat nor similar to the egg substance described by Hathaway. It is worth examining therefore what kind of part ...
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    [s.l.] : Nature Publishing Group
    Nature 217 (1968), S. 1053-1054 
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Fig. 1. Comparison of amino-acid composition among several structural proteins. 1, Rabbit actin6; 2, bacterial flagellin7; 3, rabbit myosin6; 4, insect actin6; 5, "tubulin"; 6, tropomyosin6; 7, acetic acid extract of Tetrahymena cilia8; 8, ethanol-insoluble fraction from 78; 9, ethanol-soluble ...
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 8 (1987), S. 76-84 
    ISSN: 0886-1544
    Keywords: flagella ; starfish spermatozoon ; proximal centriole ; bend direction ; bend asymmetry ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Since starfish spermatozoa have spherical heads, it is not easy to determine the topographical relationship of the axoneme to the directions of the flagellar bends, the principal, and the reverse bends as defined by Gibbons and Gibbons [J. Cell. Biol. 1972, 63:970-985]. The demembranated spermatozoa are known to take the quiescent “cane” shape with a sharp principal bend at the proximal region of the flagellum in the presence of high concentration of Ca2+. When such spermatozoa were placed on a grid for electron microscopy, fixed with osmic acid vapor, washed with distilled water, and negatively stained with urany1 acetate, the head of the spermatozoon was disrupted and dispersed disclosing the proximal centriole at at the proximal end of the flagellum. The proximal centriole was always found on the concave side of the “cane” -shaped flagella. Electron microscopy of the serial thin sections of intact and demembranated spermatozoa revealed that the doublet microtobules numbers 5 and 6 were contained in the convex edge of the principal bend.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 15 (1990), S. 168-180 
    ISSN: 0886-1544
    Keywords: microtubule-associated proteins (MAPs) ; taxol ; oocyte maturation ; fertilization ; cell division ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: A microtubule-binding protein was purified from eggs of the starfish, Asterias amurensis, through several steps of purification including the taxol-dependent procedure [Vallee, 1982, J. Cell Biol. 92:435-442]. This protein consists of a single polypeptide chain having an apparent molecular mass of 70 kD determined by SDS-PAGE. The 70 kD protein was identified as a unique microtubulebinding protein, judging from electrophoretic mobility, cleavage pattern by limited proteolysis, heat stability, and immunocrossreactivity. The 70 kD protein binds to brain and egg microtubules. It does not promote assembly of brain tubulin, but promotes that of egg tubulin in vitro in a concentration-dependent manner.Using indirect immunofluorescence and immunoelectron microscopy with the anti-70 kD protein antibody, we analyzed the cellular localization of the 70 kD protein in starfish oocytes and eggs during both meiotic maturation (meicsis) and first cleavage (mitosis). Immunofluorescence studies showed that the 70 kD protein localized on microtubule structures spread widely throughout the cytoplasm, the sperm aster, and the microtubules making up the mitotic apparatus through both meiosis and mitosis. The antibody, however, did not recognize sperm axonemes. These results were confirmed by immunoelectron microscopy. Using a colloidal gold technique, the 70 kD protein was localized along the microtubules in vivo.This 70 kD protein is the first microtubule-binding protein that has been shown to localize along the microtubules in oocytes and eggs throughout meiosis and mitosis and to promote microtubule assembly. The 70 kD protein may be involved in the dynamic changes of microtubule structures occurring within oocytes and eggs.
    Additional Material: 11 Ill.
    Type of Medium: Electronic Resource
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  • 5
    Electronic Resource
    Electronic Resource
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 2 (1982), S. 143-147 
    ISSN: 0886-1544
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Additional Material: 1 Ill.
    Type of Medium: Electronic Resource
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  • 6
    Electronic Resource
    Electronic Resource
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 10 (1988), S. 506-517 
    ISSN: 0886-1544
    Keywords: axoneme ; spokehead ; dynein ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: A high-molecular-weight polypeptide, named B-band, was partially purified from sea urchin sperm flagella using selective extraction, hydroxylapatite chromatography, and sucrose density gradient centrifugation. The molecular weight of the B-band was 440,000 by continuous system of sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE). Sedimentation coefficient of the B-band protein was 10.5 S, and its Stokes radius was 10 nm. When examined by low-angle rotary shadowing electron microscopy, this molecule appeared to be composed of four globular heads and two curved linkers (“double headphone shape”), which was quite different from the shape of 21 S dynein, the outer arm dynein. Flagellar axonemes were also subjected to several chemical dissections. The B-band was not extracted with treatments that remove both arm structures but was solubilized with treatments that extract other components such as radial spokes and nexin links. The B-band protein in the axoneme was also more susceptible to trypsin digestion than the arm structures. These results suggest that the B-band protein is a “double headphone-shaped” component of the axonemal structures and makes up the elastic structure that might regulate the active sliding between adjacent doublet microtubules.
    Additional Material: 10 Ill.
    Type of Medium: Electronic Resource
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  • 7
    ISSN: 1040-452X
    Keywords: Motility inhibitor ; Demembranated reactivated spermatozoa ; Seminal plasma ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: A sperm motility inhibitor from boar seminal plasma was purified. The purification procedure included dialysis against 0.1 M Tris-HCl containing 0.1 mM DTT and chromatographies on SP-Sephadex C-25 and Phenyl-Sepharose CL-4B. With this procedure, the seminal plasma motility inhibitor (SPMI) preparation was highly purified with a 18% recovery of inhibitory activity. The molecular weight of SPMI in native conditions has been estimated at 50,000 by molecular sieving, but 3 polypeptides with molecular weights of 14,000, 16,000 and 18,000 were observed following polyacrylamide gel electrophoresis in denaturing conditions. SPMI is a thermolabile basic protein that is stable between pH 6 and pH 11. The observations that SPMI effects on motility of demembranated spermatozoa are reversed by Mg.ATP and that SPMI inhibited bull dynein ATPase in a concentration-dependent manner suggest that this protein blocks the motility of demembranated spermatozoa by interfering with dynein arm function.
    Additional Material: 10 Ill.
    Type of Medium: Electronic Resource
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  • 8
    ISSN: 0148-7280
    Keywords: lysin ; protease inhibitor ; sea urchin ; vitelline coat ; fertilization ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: To search the spermatozoa of sea urchins for their lysins, the eggs were inseminated in the presence of various protease inhibitors. Among them, two chymotrypsin-specific inhibitors, chymostatin and N-tosyl-L-phenylalanyl-chloro-methane, as well as p-nitrophenyl p′-guanidinobenzoate, inhibit fertilization of the sea urchins, Hemicentrotus pulcherrimus and Strongylocentrotus intermedius.A chymotrypsin-like protease is presumed to be a lysin of the sea urchins, since the inhibition of fertilization by chymostatin is remarkably diminished if the eggs are pretreated with trypsin or chymotrypsin to break the vitelline coat before insemination, and since N-tosyl-L-phenylalanyl-chloromethane, and p-nitrophenyl p′-guanidinobenzoate, as well as chymostatin, inhibit the fertilization.In all the sea urchins so far studied, elevation of fertilization envelopes is inhibited by leupeptin, antipain, soybean trypsin inhibitor, and p-nitrophenyl p′-guanidinobenzoate, all of which are potent trypsin inhibitors.Synthetic inhibitors have cytotoxic side effects on the eggs, but the microbial and plant inhibitors have no such effects.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
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  • 9
    Electronic Resource
    Electronic Resource
    New York, NY : Wiley-Blackwell
    Gamete Research 13 (1986), S. 185-197 
    ISSN: 0148-7280
    Keywords: flagellar movement ; human spermatozoa ; viscosity ; cervical mucus ; hyaluronic acid ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Flagellar movement of human spermatozoa held by their heads with a micropipette was recorded by means of a video-strobe system. Spermatozoa were studied in normal Hanks' solution, Hanks' solution with increased viscosity, cervical mucus, and hyaluronic acid.When flagellar movement in normal Hanks' solution was observed from the direction parallel to the beating plane, segments of the flagellum in focus did not lie on a straight line but on two diverging dashed lines. The distance between the two dashed lines was about 20% of the bend amplitude in the major beating plane. These observations indicate that flagellar beating of human spermatozoa in normal Hanks' solution is not planar. In contrast, segments of the flagellum in focus lay on a straight line when the spermatozoa were observed in Hanks' solution with increased viscosity, cervical mucus, or hyaluronic acid. In normal Hanks' solution, free swimming spermatozoa rotated constantly around their longitudinal axes with a frequency similar to the beat frequency, whereas little or no rotation of spermatozoa occurred in Hanks' solution with increased viscosity, in cervical mucus, or in hyaluronic acid.We conclude that human spermatozoa in normal Hanks' solution beat with a conical helical waveform having an elliptical cross section, the semiaxes of which have a ratio of 0.2. The three-dimensional geometry of the flagellar movement is responsible for the rotation of the sperm around their longitudinal axes.
    Additional Material: 8 Ill.
    Type of Medium: Electronic Resource
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