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  • 1
    Electronic Resource
    Electronic Resource
    Microinjection of inositol 1,2-(cyclic)-4,5-trisphosphate, inositol 1,3,4,5-tetrakisphosphate, and inositol 1,4,5-trisphosphate into intact Xenopus oocytes can induce membrane currents independent of extracellular calcium (1989)
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 40 (1989), S. 321-330 
    Details
    ISSN: 0730-2312
    Keywords: inositol phosphates ; chloride channel ; depolarization ; membrane potential ; second messengers ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Inositol phosphate action in an intact cell has been investigated by intracellular microinjection of eight inositol phosphate derivatives into Xenopus laevis oocytes. These cells have calcium-regulated chloride channels but do not have a calcium-induced calcium release system. Microinjection of inositol 1,3,4,5-tetrakisphosphate (IP4), inositol 1,2-(cyclic)-4,5-trisphosphate (cIP3), inositol 1,4,5-trisphosphate (IP3), or inositol 4,5-bisphosphate [(4,5)IP2], open chloride channels to induce a membrane depolarization. However, inositol 1-phosphate (IP1), inositol 1,3,4,5,6-pentakisphosphate (IP5), inositol 1,4-bisphosphate, or inositol 3,4-bisphosphate are unable to induce this depolarization. The depolarization is mimicked by calcium microinjection, inhibited by EGTA coinjection, and is insensitive to removal of extracellular calcium. By means of the depolarization response, the efficacy of various inositol phosphate derivatives are compared. IP3 and cIP3 induce similar half-maximal, biphasic depolarization responses at an intracellular concentration of approximately 90 nM, whereas IP4 induces a mono- or biphasic depolarization at approximately 3400 nM. At concentrations similar to that required for IP3 and cIP3, (4,5)IP2 induces a long-term (greater than 40 min) depolarization. The efficacy (cIP3 = IP3 = (4,5)IP2 ≫ IP4) and action of the various inositol phosphates in an intact cell and their inability to induce meiotic cell division are discussed.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jcb.240400308
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  • 2
    Electronic Resource
    Electronic Resource
    Implementation of the gas chromatographic/mass spectrometric peptide sequencing program PEPALG on a personal computer for off-line analysis (1986)
    Chichester : Wiley-Blackwell
    Biological Mass Spectrometry 13 (1986), S. 343-346 
    Details
    ISSN: 1052-9306
    Keywords: Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: The gas chromatographic/mass spectrometric peptide sequencing program PEPALG has been implemented in both FORTRAN and PASCAL on a personal computer for convenient off-line analysis. The availability of PEPALG in a microcomputer-based version of both FORTRAN and PASCAL should now allow ready access to this powerful protein sequencing technique by any interested laboratory.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bms.1200130705
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  • 3
    Electronic Resource
    Electronic Resource
    The male reproductive tract of the Sciuridae (1932)
    New York, NY [u.a.] : Wiley-Blackwell
    American Journal of Anatomy 51 (1932), S. 89-155 
    Details
    ISSN: 0002-9106
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Additional Material: 16 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/aja.1000510105
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  • 4
    Electronic Resource
    Electronic Resource
    Extraction of membrane proteins by differential solubilization for separation using two-dimensional gel electrophoresis (1998)
    Weinheim : Wiley-Blackwell
    Electrophoresis 19 (1998), S. 837-844 
    Details
    ISSN: 0173-0835
    Keywords: Membrane proteins ; Solubility ; Two-dimensional polyacrylamide gel electrophoresis ; Proteome ; Escherichia coli ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: We describe the extraction and enrichment of membrane proteins for separation by two-dimensional polyacrylamide gel electrophoresis (2-D PAGE) after differential solubilization of an Escherichia coli cell lysate. In a simple three-step sequential solubilization protocol applicable for whole cell lysates, membrane proteins are partitioned from other cellular proteins by their insolubility in solutions conventionally used for isoelectric focusing (IEF). As the first step, Tris-base was used to solubilize many cytosolic proteins. The resultant pellet was then subjected to conventional solubilizing solutions (urea, 3-[(3-cholamidopropyl)dimethylammonio]-1-propanesulfonate, dithiothreitol, Tris, carrier ampholytes). Following the completion of this step, 89% of the initial E. coli sample mass was solubilized. Finally, the membrane protein rich pellet was partially solubilized using a combination of urea, thiourea, tributyl phosphine and multiple zwitterionic surfactants. Using N-terminal sequence tagging and peptide mass fingerprinting we have identified 11 membrane proteins from this pellet. Two of these outer membrane proteins (Omp), OmpW and OmpX, have previously been known only as an open reading frame in E. coli, while OmpC, OmpT and OmpTOLC have not previously been identified on a 2-D gel. The prefractionation of an entire cell lysate into multiple fractions, based on solubility, results in simplified protein patterns following 2-D PAGE using broad-range pH 3.5-10 immobilized pH gradients (IPGs). Additional advantages of sample prefractionation are that protein identification and gel matching, for database construction, is a more manageable task, the procedure requires no specialized apparatus, and the sequential extraction is conducted in a single centrifuge tube, minimizing protein loss.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.1150190539
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  • 5
    Electronic Resource
    Electronic Resource
    Insulin-like growth factor 1, insulin, and progesterone induce early and late increases in Xenopus oocyte sn-1, 2-diacylglycerol levels before meiotic cell division (1991)
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Cellular Physiology 149 (1991), S. 252-259 
    Details
    ISSN: 0021-9541
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: After a 3 to 6 hour incubation, addition of progesterone (the most effective), insulin-like growth factor 1 (IGF-1; the second most effective), or insulin induces meiotic cell division in Xenopus oocytes. Measurement of an endogenous activator of protein kinase C, sn-1,2-diacylglycerol (DAG), by an enzymatic method recording mass demonstrates that all three hormones alter DAG levels. Five seconds after addition, only progesterone transiently reduces DAG levels by about 25%. At 15 minutes after addition, all three hormones produce a peak of DAG (115% to 160% of control values), with the more effective hormones producing a larger increase in DAG. Insulin produces the smallest DAG increase, but the DAG release is longer lasting. Finally, all three hormones induce a second peak in DAG levels just before white spot appearance (at 0.85 GVBD50, where 1.0 GVBD50 is when 50% of the cells have divided). With these data and since an activator of protein kinase C, a phorbol ester, has been found to induce meiosis, the kinase may play a role in early proliferative events at the plasma membrane and in late events at the nucleus.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jcp.1041490211
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  • 6
    Electronic Resource
    Electronic Resource
    Analysis of the 13C and 1H spectra of mixtures of benzylidene derivatives (1994)
    Chichester : Wiley-Blackwell
    Organic Magnetic Resonance 32 (1994), S. 496-498 
    Details
    ISSN: 0749-1581
    Keywords: NMR ; 1H NMR ; 13C NMR ; Benzylidene derivatives ; Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: The 1H and 13C NMR spectra of methyl (E)-2,3,-diphenylprop-2-enoate and methyl (E)-2-(2-phenylethenyl) benzoate resulting from the electrocyclic ring opening of benzocyclobutenone starting materials have been assigned. A combination of direct detection 2D NMR techniques, COSY, HETCOR and FLOCK, provided the assignments of the 1H and 13C resonances.
    Additional Material: 1 Tab.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/mrc.1260320812
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  • 7
    Electronic Resource
    Electronic Resource
    A shock-tube study of the kinetics of reaction of hydroxyl radicals with H2, CO, CH4, CF3H, C2H4, and C2H6 (1976)
    New York, NY : Wiley-Blackwell
    International Journal of Chemical Kinetics 8 (1976), S. 549-561 
    Details
    ISSN: 0538-8066
    Keywords: Chemistry ; Physical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Concentration-time profiles have been measured for hydroxyl radicals generated by the shock-tube decomposition of hydrogen peroxide in the presence of a variety of additives. At temperatures close to 1300°K the rate constants for the reaction \documentclass{article}\pagestyle{empty}\begin{document}$${\rm OH} + {\rm RH} \to {\rm R} + {\rm H}_{\rm 2} {\rm O}$$\end{document} are found to be in the ratio 0.18:0.19:0.59:1.00:2.33:2.88 for the additives CO:CF3H:H2:CH4:C2H4:C2H6, respectively.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/kin.550080409
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  • 8
    Electronic Resource
    Electronic Resource
    Establishment of the human reflex tear two-dimensional polyacrylamide gel electrophoresis reference map: New proteins of potential diagnostic value (1997)
    Weinheim : Wiley-Blackwell
    Electrophoresis 18 (1997), S. 2811-2815 
    Details
    ISSN: 0173-0835
    Keywords: Two-dimensional polyacrylamide gel electrophoresis ; Tears ; Proteome ; Cancer ; Tag Sequencing ; Amino acid analysis ; Lacryglobin ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: To understand the changes in protein expression associated with various physiological states as well as the development of pathological eye disease, we have begun to map the protein components of normal human reflex tears. An analytical reference map of normal human reflex tears was created using two-dimensional polyacrylamide gel electrophoresis (2-D PAGE) with pH 3.5-10 immobilized pH gradients (IPGs). Micropreparatively loaded gels were transferred to polyvinylidene difluoride (PVDF) and analysed by a combination of N-terminal sequence tagging and amino acid compositional analysis. Thirty spots were sequence tagged, resulting in identification of six different proteins (lipocalin, lysozyme, lactotransferrin, zinc-α-2 glycoprotein, cystatin S, cystatin SN) that matched to entries in the SWISS-PROT database. A group of N-terminally blocked proteins was clearly identified from SWISS-PROT by amino acid analysis, isoelectric point (pI) and molecular weight (Mr). A number of highly expressed protein components remain unidentified despite being subjected to amino acid analysis and Edman sequencing. A majority of the abundant proteins showed varying degrees of charge heterogeneity attributed to post-translational processing such as glycosylation and N-terminal truncation. We have identified a previously undescribed protein that we have named lacryglobin. This protein displays strong homology with mammaglobin, a protein overexpressed in breast cancer. The discovery of this homologue in tears offers the potential for disease diagnosis by screening tear fluid proteins.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.1150181516
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  • 9
    Electronic Resource
    Electronic Resource
    Improved protein solubility in two-dimensional electrophoresis using tributyl phosphine as reducing agent (1998)
    Weinheim : Wiley-Blackwell
    Electrophoresis 19 (1998), S. 845-851 
    Details
    ISSN: 0173-0835
    Keywords: Tributyl phosphine ; Two-dimensional polyacrylamide gel electrophoresis ; Immobilized pH gradients ; Solubility ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: In this study, dithiothreitol was replaced by tributyl phosphine as the reducing agent in both the sample solution for the first-dimensional isoelectric focusing and during the immobilised pH gradient (IPG) equilibration procedure. Tributyl phosphine improves protein solubility during isoelectric focusing, which results in shorter run times and increased resolution. Tributyl phosphine is nonionic and thus does not migrate in the IPG, therefore maintaining reducing conditions during the course of the first-dimensional separation. The increased solubility provided by the maintenance of reducing conditions gives improved focusing and decreased horizontal streaking on the subsequent second-dimension gel. The use of tributyl phosphine in the equilibration step allows the procedure to be simplified, incorporating reduction and alkylation in a single step. This is possible because, in direct contrast to dithiothreitol (DTT), tributyl phosphine does not contain a free thiol and therefore does not react with thiol-specific alkylating reagents.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.1150190540
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  • 10
    Electronic Resource
    Electronic Resource
    The Australian proteome analysis facility (APAF): Assembling large scale proteomics through integration and automation (1998)
    Weinheim : Wiley-Blackwell
    Electrophoresis 19 (1998), S. 1883-1890 
    Details
    ISSN: 0173-0835
    Keywords: Two-dimensional polyacrylamide gel electrophoresis ; Proteome ; Robotics ; Protein identification ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: The field of proteomics opens new possibilities for the mass screening of proteins from many different sources. While genomics is well understood to be a big science field, proteomics is just emerging as such. This paper describes the setting up of the first national proteomics facility. The facility has been funded by the Australian government and this funding has allowed the design of purpose built, integrated laboratories with state of the art equipment for large scale proteome research.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.1150191106
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