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  • Analytical Chemistry and Spectroscopy  (34)
  • Life and Medical Sciences  (27)
  • Wiley-Blackwell  (61)
  • American Meteorological Society
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  • Wiley-Blackwell  (61)
  • American Meteorological Society
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  • 1
    Electronic Resource
    Electronic Resource
    Vitrification of mouse oocytes: Improved rates of survival, fertilization, and development to blastocysts (1991)
    New York, NY [u.a.] : Wiley-Blackwell
    Molecular Reproduction and Development 29 (1991), S. 373-378 
    Details
    ISSN: 1040-452X
    Keywords: Oocyte cryopreservation ; Dilution lysis ; Cooling ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Rall and Fahy's (1985) vitrification procedure for the cryopreservation of 8-cell embryos was applied to unfertilized mouse oocytes. Unchanged, this method resulted in a mean of 24.1% of vitrified oocytes fertilizing and developing to blastocysts in vitro. Exposure of oocytes to the cryoprotectant media, but without the vitrification, resulted in 30.8% developing to blastocysts. Modifications to the durations of and media used in the dilution and equilibration steps of the procedure produced a final protocol giving a mean of 55.4% of vitrified oocytes and 72.4% of nonvitrified VS1-exposed oocytes developing to blastocysts; 85.7% of control oocytes develop to blastocysts. Osmotically induced damage was found to be the most important cause of loss of viability in these methods. Cooling of oocytes to 5-8°C during the procedure had no significant effect on their viability. No parthenogenetic activation of oocytes occurred as a result of exposure to the procedure.
    Additional Material: 2 Tab.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/mrd.1080290409
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  • 2
    Electronic Resource
    Electronic Resource
    Vitrification of mouse oocytes using short cryoprotectant exposure: Effects of varying exposure times on survival (1992)
    New York, NY [u.a.] : Wiley-Blackwell
    Molecular Reproduction and Development 33 (1992), S. 210-214 
    Details
    ISSN: 1040-452X
    Keywords: Oocytes cryopreservation ; Vitrification ; Mouse ; Minimal cryoprotectant exposure ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The effects on oocyte viability of varying the duration of exposure to cryoprotectants before rapid cooling to - 196°C were examined, using the vitrification protocol of Nakagata. A very short exposure (15 sec) was found to be optimal, resulting in an overall rate of development from vitrified oocytes to hatching blastocysts of 31.8%. Very high rates of survival (77-89%) of oocytes exposed to the cryoprotectant media, but without the vitrification, together with extreme variability in results between straws in the vitrified groups, suggest that losses in viability during vitrification may result from ice damage during devitrification of the medium. (c) 1992 Wiley-Liss, Inc.
    Additional Material: 1 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/mrd.1080330214
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  • 3
    Electronic Resource
    Electronic Resource
    Endoplasmic microtubules connect the advancing nucleus to the tip of legume root hairs, but F-actin is involved in basipetal migration (1987)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 8 (1987), S. 27-36 
    Details
    ISSN: 0886-1544
    Keywords: nuclear migration ; microtubules ; F-actin ; root hairs ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: A prominent feature of tip growth in filamentous plant cells is that the nucleus often migrates in step with the tip as it extends. We have studied this long-recognized but unexplained relationship in root hairs of the legume Vicia hirsuta by a variety of microscopic techniques. Using rhodaminyl lysine phallotoxin, and antitubulin antibodies, root hairs are shown to contain axial bundles of F-actin and a complex microtubular system. To the basal side of the nucleus the microtubules are cortical and net axial but in the region between nucleus and tip the arrangement is more complicated. Electron microscopic thin sections demonstrate that internal bundles of microtubles exist in addition to the plasma membrane-associated kind. Computerized deblurring of through-focal series of antitubulin stained hairs clarifies the three-dimensional organization: bundles of endoplasmic microtubules progress from the nuclear region toward the apical dome where they can be seen to fountain out upon the cortex.The relationship between nucleus and tip can be uncoupled with antimicrotubule herbicides. Time lapse video microscopy shows that these agents cause the nucleus to migrate toward the base. This contrary migration can be inhibited by adding cytochalasin D, which fragments the F-actin bundles.It is concluded that microtubules connect the nucleus to the tip but that F-actin is involved in basipetal migration as is known to occur when symbiotic bacteria uncouple the nucleus from the tip.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/cm.970080105
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  • 4
    Electronic Resource
    Electronic Resource
    Fimbrin localized to an insoluble cytoskeletal fraction is constitutively phosphorylated on its headpiece domain in adherent macrophages (1993)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 25 (1993), S. 223-233 
    Details
    ISSN: 0886-1544
    Keywords: actin-bundling protein ; phosphorylation ; macrophage fractions ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: The actin-bundling protein fimbrin is homologous to l-plastin, a 65kD phosphoprotein expressed in leukocytes and transformed cells [de Arruda et al., J. Cell Biol. 111, 1069-1080]. Because fimbrin is present in cell adhesion sites, we studied the phosphorylation state of fimbrin and its distribution in macrophages sequentially extracted with Triton-X-100 (soluble fraction), Tween 40-deoxy-cholate (cytoskeletal fraction), and SDS (insoluble cytoskeletal fraction). The approximate distribution of fimbrin and actin among these fractions was found to be: 65% fimbrin/55% actin in the soluble fraction, 30% fimbrin/20% actin in the cytoskeletal fraction, and 5% fimbrin/25% actin in the insoluble cytoskeletal fraction. PMA did not alter this distribution. Fluorescence microscopy of acetone-extracted macrophages showed that actin is concentrated in podosomes at the substratum interface and is diffusely distributed throughout the remainder of the cell. Fimbrin colocalizes with actin in podosomes and also exhibits a punctate distribution in the cytoplasm that overlaps with actin. In Tween 40/DOC-extracted cells, podosomes remain, and fimbrin also exhibits a punctate distribution along actin filaments. Metabolic 32PO4 labeling revealed that fimbrin is constitutively phosphorylated and that phosphorylated fimbrin is concentrated in the insoluble cytoskeletal fraction. PMA increased the relative levels of fimbrin phosphorylation twofold but did not alter the pattern of fimbrin fluorescence or the distribution of phosphorylated fimbrin. Limited trypsin digestion and phosphoamino acid analysis demonstrated that phosphorylation occurs specifically on serine residues within the 10kD headpiece domain of fimbrin. Phosphorylation of the headpiece domain could regulate the actin binding and bundling properties of fimbrin, or it could regulate the interaction of fimbrin with other proteins. © 1993 Wiley-Liss, Inc.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/cm.970250303
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  • 5
    Electronic Resource
    Electronic Resource
    Effect of analyte reactivity on the capillary supercritical fluid chromatography of organophosphines (1991)
    Weinheim : Wiley-Blackwell
    Journal of High Resolution Chromatography 14 (1991), S. 127-133 
    Details
    ISSN: 0935-6304
    Keywords: Supercritical fluid chromatography ; tri(n-alkyl)phosphines ; On-column reaction ; Autoxidation ; Isomeric separation ; Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Additional Material: 12 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jhrc.1240140212
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  • 6
    Electronic Resource
    Electronic Resource
    Degradation and regeneration of the cross-linking agent azo-t-butane (1992)
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Microcolumn Separations 4 (1992), S. 221-225 
    Details
    ISSN: 1040-7685
    Keywords: Azo-t-butane ; cross-linking ; immobilization ; capillary columns ; Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: The ability of commercially available azo-t-butun (ATB) to facilitate immobilization of polysiloxane stationary phases in capillary columns deteriorates upon storage. Aged ATB produces columns with high bleed, solute retention shifts, erratic immobilization efficiency, and high activity. This deterioration is accelerated in the presence of light, suggesting free radical processes are involved. The loss of certain lowlevel impurities, which act as free radical transfer agents or radical sinks, may be responsible for the performance change. Regeneration can often temporarily be accomplished using platinum catalyzed reduction with trichlorosilane. The addition of small amounts of toluene or other radical transfer agents to aged ATB moderates the cross-linking process, allowing the reproducible production of columns with good immobilization efficiency, excellent intertness, low thermal bleed, and proper polarity.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/mcs.1220040307
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  • 7
    Electronic Resource
    Electronic Resource
    The effect of temperature on selectivity in capillary SFC (1992)
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Microcolumn Separations 4 (1992), S. 215-220 
    Details
    ISSN: 1040-7685
    Keywords: retention index ; supercritical fluid chromatography ; selectivity ; temperature ; Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Retention indices (RI) for a variety of probe compounds were determined on 50-μm i. d. columns coated with eight different stationary phases under density programmed SFC conditions at isothermal temperatures of 80 and 150°C. RI values were strongly dependent on temperature for polar probes on the polar phases containing high levels of cyanopropyl or polyethylene glycol (PEG) functionality. A lower apparent polarity was observed for polar columns at higher temperatures. Moderate RI differences were apparent with the same probes on columns with polarizable stationary phases of high phenyl or biphenyl content. Nonpolar alkyl substituted stationary phases showed only a slight temperature dependence on RI for all test compounds. Alkanes of lower molecular weight eluted at lower densities on all columns when the temperature was raised because of the contribution of volatility to elution in SFC. This same effect was observed for the higher alkanes on both nonpolar and PEG columns, but they eluted at similar densities on cyanopropyl columns and at higher densities on columns with polarizable phases when the temperature was raised. Temperature controlled selectivity tuning is a useful tool in optimizing separations in SFC.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/mcs.1220040306
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  • 8
    Electronic Resource
    Electronic Resource
    Mass spectra of some specifically deuterated tryptamines (1977)
    Chichester : Wiley-Blackwell
    Biological Mass Spectrometry 4 (1977), S. 348-353 
    Details
    ISSN: 1052-9306
    Keywords: Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: The mass spectra of the four tryptamine derivatives, N-acetyl-5-methoxytryptamine (melatonin), N-acetyl-5-hydroxytryptamine (N-acetyl-serotonin), N,N-dimethyl-5-hydroxytryptamine (bufotenine) and N,N-dimethyl-5-methoxytryptamine (O-methylbufotenine), with specifically labeled [D4]aminoethyl sidechains have been measured. Comparison of these spectra with those of the unlabeled compounds enable the major fragmentations of the compounds to be defined.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bms.1200040605
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  • 9
    Electronic Resource
    Electronic Resource
    The synthesis of α,α,β,β-d4-serotonin (1976)
    Chichester : Wiley-Blackwell
    Biological Mass Spectrometry 3 (1976), S. 146-148 
    Details
    ISSN: 1052-9306
    Keywords: Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: α,α,β,β-d4-Serotonin (94% d4, 6% d3) has been synthesized for use as an internal standard in mass spectrometric determinations of serotonin in biological systems.
    Additional Material: 1 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bms.1200030310
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  • 10
    Electronic Resource
    Electronic Resource
    Structural elucidation of the O-specific antigen of Yersinia ruckerii by fast atom bombardment mass spectrometry (FAB-MS) (1990)
    Chichester : Wiley-Blackwell
    Biological Mass Spectrometry 19 (1990), S. 787-790 
    Details
    ISSN: 1052-9306
    Keywords: Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bms.1200191207
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