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  • Chemistry  (8)
  • Amino acid sequence  (3)
  • X-ray crystallography  (3)
  • Escherichia coli  (2)
  • Histamine  (2)
Source
Material
Years
Keywords
  • 1
    Electronic Resource
    Electronic Resource
    Crystallization and Preliminary X-ray Analysis of γ-Glutamyltranspeptidase from Escherichia coli K-12
    Amsterdam : Elsevier
    Journal of Molecular Biology 234 (1993), S. 1259-1262 
    Details
    ISSN: 0022-2836
    Keywords: Escherichia coli ; X-ray crystallography ; crystallization ; glutathione ; γ-glutamyltranspeptidase
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1006/jmbi.1993.1677
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  • 2
    Electronic Resource
    Electronic Resource
    Crystallization and Preliminary X-ray Analysis of Copper Amine Oxidase from Escherichia coli K-12
    Amsterdam : Elsevier
    Journal of Molecular Biology 238 (1994), S. 635-637 
    Details
    ISSN: 0022-2836
    Keywords: Escherichia coli ; X-ray crystallography ; copper-amine oxidase ; crystallization ; monoamine oxidase
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1006/jmbi.1994.1321
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    Macrophage colony-stimulating factor purified from normal human urine Amino-terminal sequence and amino acid composition
    Amsterdam : Elsevier
    FEBS Letters 222 (1987), S. 341-344 
    Details
    ISSN: 0014-5793
    Keywords: (Human urine) ; Amino acid sequence ; Colony-stimulating factor ; Macrophage
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Physics
    Type of Medium: Electronic Resource
    URL: http://linkinghub.elsevier.com/retrieve/pii/0014-5793(87)80398-8
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  • 4
    Electronic Resource
    Electronic Resource
    Complete amino acid sequence of boar protamine
    Amsterdam : Elsevier
    Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular 744 (1983), S. 141-146 
    Details
    ISSN: 0167-4838
    Keywords: (Boar sperm nucleus) ; Amino acid sequence ; Protamine ; Sequence homology
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Type of Medium: Electronic Resource
    URL: http://linkinghub.elsevier.com/retrieve/pii/0167-4838(83)90083-3
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    Paper (German National Licenses)
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  • 5
    Electronic Resource
    Electronic Resource
    Structural study of the 1:2 methanol complex of 1,1,2,2-tetrakis(4-Hydroxyphenyl)ethane
    Amsterdam : Elsevier
    Tetrahedron Letters 34 (1993), S. 4805-4806 
    Details
    ISSN: 0040-4039
    Keywords: Tetrakis(hydroxyphenyl)ethane ; X-ray crystallography ; ^1^3C CP/MAS NMR ; hydrogen bond ; inclusion complex
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://linkinghub.elsevier.com/retrieve/pii/S0040-4039(00)74093-7
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  • 6
    Electronic Resource
    Electronic Resource
    Direct and indirect effects of histamine on the smooth muscle cells of the guinea-pig main pulmonary artery (1983)
    Springer
    Pflügers Archiv 399 (1983), S. 46-53 
    Details
    ISSN: 1432-2013
    Keywords: Histamine ; Main pulmonary artery ; Neuromuscular transmission ; Noradrenaline sensitivity
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Electrophysiological studies of the effects of histamine on the smooth muscles in the guinea-pig main pulmonary artery revealed that this amine produced muscle contraction with an associated depolarization of the membrane. Application of cimetidine potentiated and that of mepyramine suppressed these histamine-induced responses. In the presence of mepyramine, histamine produced membrane hyperpolarization. Contractions produced by perivascular nerve stimulation were potentiated by histamine, and additional application of cimetidine further potentiated while addition of mepyramine suppressed the histamine-induced enhancement. The amplitude of excitatory junction potentials was increased by application of histamine plus cimetidine and was decreased by histamine plus mepyramine. Excitatory effects of histamine on the electrical and mechanical responses were reduced by application of tetrodotoxin, prazosin, phentolamine or guanethidine. In the presence of these drugs, histamine produced depolarization with an associated increase in membrane resistance and, in high concentrations, produced spike potentials. Electrical and mechanical responses of the smooth muscles to exogenously applied noradrenaline were potentiated by pretreatment with histamine and cimetidine, and were suppressed by histamine and mepyramine. These observations indicate that the guinesa-pig main pulmonary artery possesses two types of histamine receptor, H1- and H2-receptors, in the smooth muscles and in the perivascular adrenergic nerves. Stimulation of H1 or H2-receptor produces excitatory or inhibitory effects, respectively, on the smooth muscles and on the adrenergic nerves. Contraction of the muscle tissues produced by histamine is brought about by a direct effect on the smooth muscles and by increased release of transmitters, as a result of excitation of perivascular nerves.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00652521
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  • 7
    Electronic Resource
    Electronic Resource
    The effect of histamine on the smooth muscle cells of the ear artery of the rabbit (1980)
    Springer
    Pflügers Archiv 387 (1980), S. 17-25 
    Details
    ISSN: 1432-2013
    Keywords: Vascular smooth muscle ; Histamine ; Excitation-contraction-coupling ; Perivascular nerves ; Cellular Ca store
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Histamine activates both H1- and H2-receptors in the ear artery of the rabbit. The specific action of these receptor activations on the membrane potential and the force development has been investigated by using the H1-blocking agent mepyramine and the H2-blocking agent cimetidine. H1-activation depolarizes and increases force development, while H2-activation hyperpolarizes and reduces force development. These effects on the force development can occur independently of the changes of the membrane potential. By determining the effect of histamine on tissues which were denervated with 6-hydroxydopamine it was shown that histamine exerts its effect directly on the smooth muscle cells. Na-deficiency depolarizes the smooth muscle cells, but it also reduces the changes of the membrane potential and the force development induced by H1-stimulation. K-free medium prevents the hyperpolarizing effect of H2-activation. As far as the ion fluxes are concerned and H1-activation is found to induce an increased efflux of K while a simultaneous H2-activation only reduces the increase of flux induced by H1-activation. H1-activation induces a release of Ca from the intracellular Ca stores, while H2-activation inhibits this release.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00580839
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  • 8
    Electronic Resource
    Electronic Resource
    Partial amino acid sequence of organ of Corti protein OCP-II (1990)
    Springer
    European archives of oto-rhino-laryngology and head & neck 248 (1990), S. 15-18 
    Details
    ISSN: 1434-4726
    Keywords: OCP-II ; Organ of Corti ; Proteins ; Amino acid sequence
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary We have previously described two low-molecular-weight, highly acidic proteins which are present in the organ of Corti in extremely high concentrations. Since the function of these proteins is not known, they have been assigned the tentative names OCP-I and OCP-II. In the hope of obtaining information about their function through homology studies, we have initiated amino acid sequencing of these proteins. We have recently succeeded in obtaining a brief amino-terminal sequence of OCP-II. We now report on a significant extension of the amino-terminal sequence of OCP-II and our first results on sequences of peptide fragments obtained by limited digestion with V8 protease. Together, the sequenced segments account for about one-third of the total sequence. Comparisons with the sequences of known proteins suggest that OCP-II is not a structural protein, but that it may exhibit biologic activity.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00634774
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  • 9
    Electronic Resource
    Electronic Resource
    Determination of the level of the core of 2′,5′-oligoadenylates by high performance liquid chromatography (1992)
    New York, NY : Wiley-Blackwell
    Biomedical Chromatography 6 (1992), S. 35-38 
    Details
    ISSN: 0269-3879
    Keywords: Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: A simple and rapid method for analysis of the core of 2′,5′-oligoadenylates, mainly based on the use of high performance liquid chromatography (HPLC), is described. Perchloric acid extracts of tissues or cells were first treated with nuclease P1. Portions of the extracts were then digested with alkaline phosphatase. HPLC analysis of the extracts was performed on a column system composed of an Ultrasphere ODS precolumn (4.6 × 45 mm) and an Ultrasphere Octyl column (4.6 × 250 mm) by stepwise elution using a 50 mM ammonium phosphate buffer, pH7, containing 3.5 and 7% methanol. Three species of the core of 2′,5′-oligoadenylates (dimer, trimer and tetramer) from a number of samples were eluted separately with 7% methanol, and the concentration of each core was directly estimated using constant values calculated with the standard core. The level of the core of 2′,5′-oligoadenylates in tissues and cells determined by our method is similar to that reported by other authors who used biological, radiobinding or radioimmunological assays.
    Additional Material: 1 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bmc.1130060110
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  • 10
    Electronic Resource
    Electronic Resource
    Preparation of immobilized enzymes by N-Vinylpyrrolidone and the general properties of the glucoamylase gel (1974)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 16 (1974), S. 1517-1528 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Immobilized glucoamylase, invertase, and β-galactosidase were prepared by using N-vinylpyrrolidone monomer (VP) under γ-ray irradiation. The enzyme-VP solutions were gelled by irradiation with 2.9 Mrad and the added enzymes were almost completely entrapped. Activity losses on entrapping were 55% for the VP-glucoamylase gel, and more than 90% in the case of VP-invertase and VP-β-galactosidase gels. No leakage of enzyme from these gels could be detected within 1 hr. The VP-glucoamylase gel was capable of hydrolyzing dextrin (mol wt 10,400) to glucose and the glucose equivalent was equal to that obtain able with native enzyme. The optimum temperature, heat stability, pH activity curve, and pH stability of VP-glucoamylase gel were slightly inferior to those of native enzyme, while Km was a little larger than that of native enzyme.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260161108
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