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  • Analytical Chemistry and Spectroscopy  (5)
  • Animals  (3)
  • 1985-1989  (8)
  • 1930-1934
  • 1
    Electronic Resource
    Electronic Resource
    Characterization of glutathione conjugates by fast atom bombardment/tandem mass spectrometry (1988)
    Chichester : Wiley-Blackwell
    Biological Mass Spectrometry 15 (1988), S. 615-621 
    Details
    ISSN: 0887-6134
    Keywords: Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: The collisionally activated decomposition of [M + H]+ ions, generated by fast atom bombardment (FAB) of glutathione conjugates, has been studied by tandem mass spectrometry (MS/MS) using hybrid sector/quadrupole instruments. Abundant fragments of diagnostic utility were present in the daughter ion spectra. Common fragmentation modes were observed but their relative importance was strongly dependent on the nature of the conjugated species. As an example of a general approach to the characterization of glutathione conjugates in biological samples, the acetaminophen-glutathione conjugate was identified in rat bile, following coadministration of (2H0)- and (2H3)acetaminophen, using the experimental sequence: (i) conventional FAB mass spectrometric analysis, (ii) MS/MS using constant neutral loss (129 u) scanning to identify parent ions corresponding to glutathione conjugates, (iii) MS/MS to yield daughter ion spectra of parents so identified and corresponding to (2H0)- and (2H3)-labeled conjugates.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bms.1200151107
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  • 2
    Electronic Resource
    Electronic Resource
    Selected reaction monitoring during gas chromatography/mass spectrometry of eicosanoids (1988)
    Chichester : Wiley-Blackwell
    Biological Mass Spectrometry 16 (1988), S. 409-413 
    Details
    ISSN: 1052-9306
    Keywords: Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Gas chromatography/electron capture negative ion mass spectrometry of eicosanoids, as pentafluorobenzyl (PFB) ester, methyl oxime (where applicable), trimethylsilyl (TMS) ether derivatives, is reported using a double-focusing instrument of trisector configuration. Sub-picogram detection limits were observed for prostaglandins E1, E2 and F2α during selected ion monitoring (SIM) of [M — PFB]- ions. Selected reaction monitoring (SRM) of [M — PFB]- → [M — PFB — TMSOH]-, occurring in the first field-free region, was of modest sensitivity, reflecting the stability of the [M - PFB]- ions. The leukotriene B4 (LTB4) derivative was successfully analyzed by SIM at the low-picogram level. In this instance, the fragmentation [M — PFB]- →[M — PFB — TMSOH] occurred in high yield in the first field-free region. The advantageous improvement in selectivity of detection that may be achieved with SRM was evident during the analysis of a serum extract for LTB4.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bms.1200160180
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  • 3
    Electronic Resource
    Electronic Resource
    Application of relayed coherence transfer two-dimensional nuclear magnetic resonance spectroscopy to the assignment of 1H chemical shifts in steroids (1988)
    Chichester : Wiley-Blackwell
    Organic Magnetic Resonance 26 (1988), S. 214-223 
    Details
    ISSN: 0749-1581
    Keywords: RELAY 2D NMR ; 1H NMR ; 2D NMR Steroids ; Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Relayed coherence transfer (RELAY) two-dimensional NMR spectroscopy was demonstrated to be an effective technique for overcoming the problem of overlapping multiplets in the analysis of the 1H NMR spectra of steroids. Cross-sections through appropriate proton resonances resulted in resolved spectra of the spin systems for each of the saturated rings of the estrogenic hormones 17β- and 17α-estradiol. During RELAY experiments with a fixed delay time of 0.042 s it was possible to observe RELAY cross-peaks between H-11α and 18-CH3 which resulted from magnetization transfer via long-range coupling between 18-CH3 and H-12α. The difference in stereochemistry at C-17 of these estradiol epimers allowed an examination of the effect of substituent configuration on the RELAY cross-peak intensity in order to determine the ability of the RELAY method to provide qualitative structural information.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/mrc.1260260308
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  • 4
    Electronic Resource
    Electronic Resource
    Identification of C-glycopyranosides and C-glycofuranosides by 13C NMR and 1H NMR. Complete assignment of their spectral data using carbon-proton chemical shift correlation spectroscopy (1988)
    Chichester : Wiley-Blackwell
    Organic Magnetic Resonance 26 (1988), S. 1062-1067 
    Details
    ISSN: 0749-1581
    Keywords: 1H ; 13C NMR 2D NMR ; C-Glycopyranosides ; C-Glycofuranosides ; Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: C-Glycopyranosides and C-glycofuranosides were identified using 13C and 1H chemical shift and coupling constant data. Full assignments for all α- and β-anomers were made possible by recourse to carbon-proton chemical shift correlation spectroscopy. Greater steric shielding effects were observed on the carbon atoms in cis-1,2-substituted compounds compared with their trans counterparts. Consistent proton chemical shift differences were also noted in that the anomeric protons resonate at lower field in all cis-1,2-isomers.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/mrc.1260261206
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  • 5
    Electronic Resource
    Electronic Resource
    NMR of the methylene group: Artifacts in the proton-proton decoupled heteronuclear two-dimensional chemical shift correlation experiment (1988)
    Chichester : Wiley-Blackwell
    Organic Magnetic Resonance 26 (1988), S. 1058-1061 
    Details
    ISSN: 0749-1581
    Keywords: Two-dimensional NMR ; Artifacts ; BIRD pulses ; Coherence transfer ; Methylene groups ; Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: When the proton-proton decoupled heteronuclear two-dimensional chemical shift correlation experiment is applied to a molecule containing methylene groups, the spectra show not only the expected signals at the two proton chemical shifts, but also a strong artifact. This artifact appears at the average of the two proton chemical shifts, and arises from coherence transfer between the two protons caused by the BIRD pulse. It is not caused by strong coupling between the protons, and so may appear in any spectrum. The dependence of this artifact on experimental conditions was analysed, and is illustrated with results obtained on the methylene groups from the cyclophane ring in N6′,N9-octamethylenepurinecyclophane.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/mrc.1260261205
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  • 6
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    The neuron-specific protein PGP 9.5 is a ubiquitin carboxyl-terminal hydrolase (1989)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1989-11-03
    Description: A complementary DNA (cDNA) for ubiquitin carboxyl-terminal hydrolase isozyme L3 was cloned from human B cells. The cDNA encodes a protein of 230 amino acids with a molecular mass of 26.182 daltons. The human protein is very similar to the bovine homolog, with only three amino acids differing in over 100 residues compared. The amino acid sequence deduced from the cDNA was 54% identical to that of the neuron-specific protein PGP 9.5. Purification of bovine PGP 9.5 confirmed that it is also a ubiquitin carboxyl-terminal hydrolase. These results suggest that a family of such related proteins exists and that their expression is tissue-specific.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wilkinson, K D -- Lee, K M -- Deshpande, S -- Duerksen-Hughes, P -- Boss, J M -- Pohl, J -- New York, N.Y. -- Science. 1989 Nov 3;246(4930):670-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, Emory University School of Medicine, Atlanta, GA 30322.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2530630" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; B-Lymphocytes/enzymology ; Base Sequence ; Cattle ; DNA/genetics ; Humans ; Isoenzymes/genetics ; Molecular Sequence Data ; Neuropeptides/*genetics/isolation & purification ; Sequence Homology, Nucleic Acid ; Thiolester Hydrolases/*genetics/isolation & purification ; Ubiquitin Thiolesterase
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 7
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    Optical image quality and the cone mosaic (1986)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1986-01-31
    Description: Contrary to the orthodox view that optical image quality should "match" the photoreceptor grain, anatomical data from the eyes of various animals suggest that the image quality is significantly superior to the potential resolution of the cone mosaic in most retinal regions. A new theory is presented to explain the existence of this relation and to better appreciate eye design. It predicts that photoreceptors are potentially visible through the natural optics.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Snyder, A W -- Bossomaier, T R -- Hughes, A -- New York, N.Y. -- Science. 1986 Jan 31;231(4737):499-501.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3941914" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cats ; Humans ; Models, Neurological ; Photoreceptor Cells/*anatomy & histology ; Rats ; Snakes ; Species Specificity ; *Vision, Ocular ; *Visual Perception
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 8
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    Point mutations in the human vitamin D receptor gene associated with hypocalcemic rickets (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-12-23
    Description: Hypocalcemic vitamin D-resistant rickets is a human genetic disease resulting from target organ resistance to the action of 1,25-dihydroxyvitamin D3. Two families with affected children homozygous for this autosomal recessive disorder were studied for abnormalities in the intracellular vitamin D receptor (VDR) and its gene. Although the receptor displays normal binding of 1,25-dihydroxyvitamin D3 hormone, VDR from affected family members has a decreased affinity for DNA. Genomic DNA isolated from these families was subjected to oligonucleotide-primed DNA amplification, and each of the nine exons encoding the receptor protein was sequenced for a genetic mutation. In each family, a different single nucleotide mutation was found in the DNA binding domain of the protein; one family near the tip of the first zinc finger (Gly----Asp) and one at the tip of the second zinc finger (Arg----Gly). The mutant residues were created in vitro by oligonucleotide directed point mutagenesis of wild-type VDR complementary DNA and this cDNA was transfected into COS-1 cells. The produced protein is biochemically indistinguishable from the receptor isolated from patients.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hughes, M R -- Malloy, P J -- Kieback, D G -- Kesterson, R A -- Pike, J W -- Feldman, D -- O'Malley, B W -- New York, N.Y. -- Science. 1988 Dec 23;242(4886):1702-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell Biology, Baylor College of Medicine, Houston, TX 77030.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2849209" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Binding Sites ; Calcitriol/metabolism ; Cell Line ; Cell Line, Transformed ; Codon ; DNA/genetics/metabolism ; Exons ; Female ; Gene Amplification ; Homozygote ; Humans ; Hypocalcemia/*genetics ; Immunoblotting ; Male ; Molecular Sequence Data ; *Mutation ; Receptors, Calcitriol ; Receptors, Steroid/*genetics/metabolism ; Rickets/*genetics ; Transfection
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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