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  • 1
    Electronic Resource
    Electronic Resource
    Phosphatidylcholine and phosphatidylinositol-specific phospholipases C of bull and rabbit spermatozoa (1992)
    New York, NY [u.a.] : Wiley-Blackwell
    Molecular Reproduction and Development 33 (1992), S. 281-286 
    Details
    ISSN: 1040-452X
    Keywords: Sperm (bull, rabbit) ; Plasma membranes ; Acrosomal membranes ; Phosphatidylinositol specific phospholipase C ; Phosphatidyl choline specific phospholipase C ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Acrosomal reaction is an essential prerequisite to fertilization. The changes in lipid composition of sperm membranes cause fusion of the plasma and outer acrosomal membranes that results in the exocytosis of acrosomal contents. We report that both bull and rabbit spermatozoa contain a phosphatidylcholine-specific phospholipase C (PC-PLC) that hydrolyzes L-α-dipalmitoyl-(choline-methyl-14C-153.0 Ci/mmol and a phosphatidyl-inositol-specific phospholipase C (Pl-PLC)) that hydrolyzes L-α-(Myo)-lnositol-2-3H (N)-5.2 Ci mmol. Pl-PLC from bull sperm acrosome has been purified 568 × fold with a specific activity 6.25 ± 0.6 nmol/min/mg protein, km 0.004 mM, and Vmax 12 nmol/min/mg protein. Both enzymes had optimum at pH 7.5. The activity of PC-PLC remained unaffected by varying concentrations of Ca2+, whereas Pl-PLC activity was significantly increased. The bulk of Pl-PLC was found to be associated with inner acrosomal membrane of bull and rabbit sperm, while PC-PLC was found in the outer acrosomal membranes in the bull sperm and the plasma membrane of the rabbit sperm. Both enzymes are compartmentalized in sperm cell. © 1992 Wiley-Liss, Inc.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/mrd.1080330308
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  • 2
    Electronic Resource
    Electronic Resource
    Phospholipids of rabbit and bull sperm membranes: Structural order parameter and steady-state fluorescence anistropy of membranes and membrane leaflets (1993)
    New York, NY [u.a.] : Wiley-Blackwell
    Molecular Reproduction and Development 35 (1993), S. 209-217 
    Details
    ISSN: 1040-452X
    Keywords: Sperm (bull, rabbit) ; Plasma membranes ; Acrosomal membranes ; Phospholipids ; Membrane fluidity ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The plasma (PM), outer acrosomal (OAM), and inner acrosomal membranes (IAM) were isolated from rabbit and bull spermatozoa and the major phospholipids characterized. Choline-containing phospholipids, phosphatidylcholine (PC) and sphingomyelin (SM), constituted more than 60% of the total phospholipids (TPL) in all membranes of both species. Approximately more than 50% of PC in membrane preparations contained some form of ether linkage. Compared to OAM and IAM, cholesterol to phospholipid molar ratio was highest in PM of both species. Contrarily, protein to phospholipid ratio for PM was lowest compared to other membranes. The sphingomyelin to phosphatidylcholine ratio increased in the direction from PM to OAM to IAM. The hydrophobic fluorescent probe 1,6-diphenyl-1,3,5-hexatriene (DPH) was used to examine both the steady-state fluorescence anisotropy parameters and structural order parameter SDPH. The data showed higher rigidity in rabbit spermatozoa compared to bull spermatozoa (SDPH = 0.7582 and SDPH = 0.7326). In both species OAM had higher rigidity compared to the other two membranes (SDPH(OAM) = 0.7809, SDPH(PM) = 0.7308, and SDPH(IAM) = 0.7481 for bull; SDPH(OAM) = 0.8091, SDPH(PM)= 0.7857, and SDPH(IAM) = 0.7663 for rabbit). The inner leaflets of bull and rabbit spermatozoal membranes had significantly higher rigidity than the outer leaflets (for inner leaflet: rabbit-SDPH(PM) = 0.8391, SDPH(OAM) = 0.8149, and SDPH(IAM) = 0.7675; bull-SDPH(PM) = 0.8000, SDPH(OAM) = 0.7990, and SDPH(IAM) = 0.7990, and for outer leaflet: rabbit-SDPH(PM) = 0.7021, SDPH(OAM) = 0.7145, and SDPH(IAM) = 0.6867; bull-SDPH(PM) = 0.6986, SDPH(OAM) = 0.5980, and SDPH(IAM) = 0.7388). © 1993 Wiley-Liss, Inc.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/mrd.1080350215
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  • 3
    Electronic Resource
    Electronic Resource
    Purification and characterization of β-glucuronidase from bull seminal plasma and its role in fertilization (1994)
    New York, NY [u.a.] : Wiley-Blackwell
    Molecular Reproduction and Development 38 (1994), S. 404-409 
    Details
    ISSN: 1040-452X
    Keywords: β-glucuronidase ; Seminal plasma ; Ovum ; Cumulus ; Fertilization ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Bull seminal plasma contains high levels of β-glucuronidase. The present study describes the isolation and characterization of β-glucuronidase, and its role in fertilization. β-glucuronidase was purified by ion exchange chromatography, saccharolactone-agarose affinity chromatography, and gel filtration. The specific activity of the purified enzyme was 4,414 μmoles/mg protein/min. The purified enzyme showed a single band on 7.5% PAGE. On SDS-PAGE, the enzyme appeared to consist of four identical subunits of Mr 75,000 each. The apparent Km and Vmax for β-glucuronidase were 0.4 mM and 5.7 μmol/min using phenolpthalein mono-β-glucuronic acid as the substrate. β-glucuronidase appeared to accelerate the cumulus dispersion in vitro. © 1994 Wiley-Liss, Inc.
    Additional Material: 8 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/mrd.1080380408
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  • 4
    Electronic Resource
    Electronic Resource
    Yeast Saccharomyces cerevisiae selectable markers in pUC18 polylinkers (1990)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 6 (1990), S. 363-366 
    Details
    ISSN: 0749-503X
    Keywords: Saccharomyces cerevisiae ; Selectable markers ; Plasmids ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: A set of plasmids was constructed that contain the yeast selectable markers HIS3, LEU2, TRP1 or URA3 embedded in the multiple cloning site of pUC18.
    Additional Material: 1 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/yea.320060502
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