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  • 1
    Electronic Resource
    Electronic Resource
    Estimation of nitrogen-15 levels in derivatized amino acids using gas chromatography quadrupole mass spectrometry with chemical ionization and selected ion monitoringAbbreviation: HFBA = heptafluorobutyric anhydride. (1978)
    Chichester : Wiley-Blackwell
    Biological Mass Spectrometry 5 (1978), S. 648-653 
    Details
    ISSN: 0306-042X
    Keywords: Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: The data indicate that a commercial, low resolution mass spectrometer can be used with chemical ionization and selected ion monitoring, without a data system, to estimate nitrogen-15 isotopic enrichment with a sensitivity and precision adequate for many biological studies. This was demonstrated using derivatized amino acid mixtures with separation and direct introduction into the mass spectrometer via a gas chromatograph. The method can discriminate between mean levels separated by 0.1 atom % 15N with 68% confidence at the 0.1 nmol level. Labeled dansylamide samples, inserted by probe, were also measured for 15N content.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bms.1200051203
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  • 2
    Electronic Resource
    Electronic Resource
    The reactions of the ions [XC]+, [X2C]+·, [X3C]+· and [X4C]+· (where X = H or F) with ethene and propene (1987)
    Chichester : Wiley-Blackwell
    Biological Mass Spectrometry 22 (1987), S. 154-156 
    Details
    ISSN: 0030-493X
    Keywords: Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: The reaction of C1 ions with ethene and propene has been studied in the gas phase using a triple quadrupole mass spectrometer.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/oms.1210220307
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  • 3
    Electronic Resource
    Electronic Resource
    Identification of some abnormal haemoglobins by fast atom bombardment mass spectrometry and fast atom bombardment tandem mass spectrometry (1988)
    Chichester : Wiley-Blackwell
    Biological Mass Spectrometry 16 (1988), S. 41-44 
    Details
    ISSN: 1052-9306
    Keywords: Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: The characterization of two abnormal human haemoglobins by fast atom bombardment (FAB) mapping is presented. The first variant, called ‘R’, exhibits a tryptic FAB map identical to that of normal haemoglobin. However, using Staphylococcus protease V8, a peptide containing the carboxyl end of the β-chain exhibits a mass shift down to 300 mass units. This clearly indicates the deletion of the two last amino acids of the β-chain. The second variant, called ‘Grenoble’, is due to two different modifications of the β-chain. The location of the Pro → Ser exchange on peptide T5 is achieved by the collisionally activated dissociation mass analyzed ion kinetic energy spectra of the corresponding [MH]+ ion. The m/z value of that peptide indicated a supplementary acid → amide modification, which was located by amino acid sequencing using chemical methods. This work concludes with the necessity of using complementary methods for achieving rapid determinations of abnormal proteins with minute amounts.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bms.1200160108
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  • 4
    Electronic Resource
    Electronic Resource
    Comparative aspects of oxidative metabolism of neutrophils from human blood and guinea pig peritonea: Magnitude of the respiratory burst, dependence upon stimulating agents, and localization of the oxidases (1980)
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Cellular Physiology 105 (1980), S. 541-551 
    Details
    ISSN: 0021-9541
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: We have compared the subcellular sites of H2O2 and presumably also superoxide-(O2-) production, and certain aspects of metabolic responses (O2 consumption, O2- production) of stimulated neutrophils from human blood and those elicited into guinea pig peritonea. Stimulation was accomplished with either opsonized zymosan or phorbol-12-myristate-13-acetate (PMA). Striking quantitative differences were observed between these cell types with regard to the increased respiration and O2- production observed during stimulation. These differences were most apparent when opsonized zymosan served as the stimulating agent. They were minimized when the soluble stimulating agent, PMA, was used. With either stimulus, the subcellular sites of H2O2 production were the same for both types of neutrophils, i.e., the plasmalemma and phagosomal membranes. No H2O2 production could be detected cytochemically in the absence of stimulation.Treatment of both unstimulated human blood and elicited guinea pig peritoneal neutrophils with the nonpenetrating, covalently linking reagent, p-diazobenzenesulfonic acid, failed to diminish O2- production upon subsequent stimulation, in contrast to a previous report. These data are discussed in terms of the possible cytological arrangements of the respiratory enzyme(s), and the different modes of stimulation of neutrophil metabolism by various agents. Ancillary data on elicited mouse peritoneal neutrophils are presented.
    Additional Material: 9 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jcp.1041050319
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  • 5
    Electronic Resource
    Electronic Resource
    Induction of alkaline phosphatase in choriocarcinoma cells by 1-β-D-arabinofuranosyl-cytosine, mitomycin C, phleomycin, and cyclic nucleotides (1977)
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Cellular Physiology 92 (1977), S. 221-231 
    Details
    ISSN: 0021-9541
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Alkaline phosphatase is induced in cultured human choriocarcinoma cells by three inhibitors of DNA synthesis which alter DNA structure: 1-β-D-arabinofuranosyl-cytosine, mitomycin C, and phleomycin. No induction is observed with the inhibitors, hydroxyurea and thymidine, which do not alter DNA structure. Cyclic AMP, analogs of cyclic nucleotides, and sodium butyrate also induce alkaline phosphatase in these cells. Among the cyclic nucleotides tested, dibutyryl cyclic AMP is the best inducer, whereas dibutyryl cyclic GMP is a poor inducer.Induction of alkaline phosphatase by inhibitors of DNA synthesis or by exposure to dibutyryl cyclic AMP appears to utilize different mechanisms. Maximum induction is observed after simultaneous addition of both types of inducers at the concentrations found to be optimal for each inducer alone. Under these conditions, the induced activity is equal to or greater than the sum of the activities induced by each inducer. RNA synthesis and protein synthesis are required for induction.Dibutyryl cyclic AMP added to cultures of choriocarcinoma cells is not degraded in the culture medium, but is extensively degraded in the cells. Nevertheless, significant amounts of dibutyryl and monobutyryl cyclic AMP are found intracellularly throughout the experiment. Since the cellular uptake of dibutyryl cyclic AMP is extremely slow, the amount of butyrate released by intracellular degradation cannot account for the observed induction. Neither the rate of uptake nor the stability of dibutyryl cyclic AMP are changed by the addition of 1-β-D-arabinofuranosyl-cytosine to the culture medium. Furthermore, 1-β-D-arabinofuranosyl-cytosine inhibits the induction by sodium butyrate. The results indicate that butyrate is not the major mediator of induction by dibutyryl cyclic AMP.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jcp.1040920210
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  • 6
    Electronic Resource
    Electronic Resource
    Comparative biochemical and cytochemical studies on superoxide and peroxide in mouse macrophages (1983)
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Cellular Physiology 115 (1983), S. 208-216 
    Details
    ISSN: 0021-9541
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Maximal rates of superoxide (O-2) release, and the cytochemical locales of peroxide staining in resident, elicited, and activated macrophages have been determined. Macrophages elicited into the peritoneum with either casein (1.2% w/v) or proteose-peptone (10.0% w/v) release about twice as much O-2 as macrophages activated by infection of the animals with either Listeria monocytogenes, or Bacille Calmette-Guerin (BCG) followed by immune boosting with Purified Protein Derivative (PPD) (i.e., about 35 vs. 14-18 nmol O-2/min/107 cells). Macrophages elicited with thioglycollate (3.0% w/v) and resident macrophages produce negligible amounts of O-2 upon stimulation with PMA. These data are compared with those reported by other investigators who used different procedures. A cytochemical procedure for localizing peroxide has been modified for use with murine macrophages. No production of H2O2 by macrophages is detected cytochemically in the absence of stimulation. Upon exposure to PMA, resident macrophages are still largely unresponsive. Approximately 20% of the casein elicited macrophages and BCG-PPD activated macrophages exhibit H2O2 staining, which is largely restricted to the cytoplasmic vesicles and channels induced by PMA in these cells. The only exception to this staining pattern is a small population (about 2%) of activated macrophages which exhibits H2O2 staining in the cytoplasmic vesicles and channels and on the plasmalemma as well.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jcp.1041150216
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