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  • 1
    Electronic Resource
    Electronic Resource
    Triadic bed-sharing and infant temperature (2002)
    Oxford, UK : Blackwell Science Ltd.
    Child 28 (2002), S. 0 
    Details
    ISSN: 1365-2214
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine , Psychology
    Notes: The effects on infants of sleeping with their parents is currently the subject of much debate. One concern regarding infants who sleep in their parents’ bed involves the possibility of overheating. Previous research reported a significantly greater core temperature of 0.1°C among a cohort of bed-sharing infants compared with a matched cohort of infants sleeping alone. This paper presents a preliminary analysis of the overnight rectal temperature of 12 of the 20 infants who were monitored sleeping alone and with their parents on separate nights at the University of Durham Parent-Infant Sleep Lab. No significant differences were found in all night rectal temperature, or temperature from 2 h after sleep onset between bed-sharing and cot sleeping nights. These preliminary analyses suggest a night-time difference in rectal temperature between routine bed-sharers and routine cot sleepers, however, these findings will be further explored in the full analyses for this study.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1365-2214.2002.00015.x
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Affinity purification of 101 residue rat cpn10 using a reversible biotinylated probe (1995)
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Peptide Science 1 (1995), S. 288-294 
    Details
    ISSN: 1075-2617
    Keywords: Stepwise SPPS ; HBTU/HOBt ; capping ; avidin-biotin ; chaperonin 10 (R. norvegicus) ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: The purification of large synthetic peptides using conventional separation techniques often results in poor yields and homogeneity due to the accumulation of chromatographically similar deletion and truncated impurities. We have developed a highly effective synthetic strategy and one-step purification procedure that is based on (i) the application of single coupling using HBTU/HOBt activation to reduce incomplete couplings, (ii) the use of N-(2-chlorobenzyloxycarbonyloxy)succinimide as a capping agent to terminate deletion sequences and (iii) the N-terminal derivatization of the complete peptidyl-resin with a reversible Fmoc-based chromatographic probe possessing enhanced physico-chemical properties (i.e. hydrophobicity, charge or affinity label). We report the application of a biotinylated probe, activated as the succinimidyl carbonate, for the purification of a 101 residue chaperonin protein from Rattus norvegicus (rat cpn10), previously synthesized using an optimized synthetic protocol. Biotinylated rat cpn10 was separated from underivatized impurities on an immobilized monomeric avidin column. Free rat cpn10 was released from avidin-agarose column with 5% aqueous triethylamine and after desalting by RP-HPLC gave 9.9% recovery. Characterization and assessment of homogeneity was achieved using ESI-MS, CZE and RP-HPLC.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/psc.310010503
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    Application of reversible biotinylated label for directed immobilization of synthetic peptides and proteins: isolation of ligates from crude cell lysates (1997)
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Peptide Science 3 (1997), S. 252-260 
    Details
    ISSN: 1075-2617
    Keywords: affinity chromatography ; avidin-biotin ; chaperonin 10 from Rattus norvegicus ; directed immobilization ; GroEL ; peptide synthesis ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Chaperonin 10 protein from Rattus norvegicus (Rat cpn10) has been reported to bind chaperonin 60 from Escherichia coli (GroEL) in an ATP-dependent manner. Chemically synthesized Rat cpn10 was immobilized in a defined orientation to agarose-bound monomeric avidin using a reversible biotinylated affinity label (1), attached to the Nα-terminal residue. The resulting affinity chromatographic matrix was then used to isolate binding proteins from a crude cell lysate. Following affinity separation the bound ligand and ligate was released by treatment with organic base. Rat cpn10 was prepared using a highly effective synthetic protocol involving HBTU/HOBt activation and capping with N-(2-chlorobenzyloxycarbonyloxy) succinimide to terminate unreacted amino groups. The biotinylated Fmoc-based molecule (1) was introduced specifically onto the Nα-terminal amino acid as the succinimidyl carbonate, before final cleavage and deprotection of side-chain protecting groups using a low-TFMSA/high-HF procedure. Crude biotinylated Rat cpn10 (Rat cpn10+1) was immobilized on monomeric avidin with a binding efficiency of approximately 75% and unlabelled truncated/capped impurities eluted off the column with buffer. The biotinylated Rat cpn10-avidin affinity matrix was then used to isolate GroEL from a crude cell lysate. The identity of the purified protein was confirmed by SDS-PAGE and binding to a specific anti-GroEL monoclonal antibody (MoAb). These results extend the applicability of the biotinylated label (1), providing a reversible non-covalent anchor for immobilization of peptide and protein ligands, thus simplifying isolation of ligates and enabling recovery of synthetic material under mild conditions. © 1997 European Peptide Society and John Wiley & Sons, Ltd.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
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    Paper (German National Licenses)
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