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  • 1990-1994  (4)
  • 1985-1989  (2)
  • 1965-1969
  • 1960-1964
  • 1935-1939
  • Chemistry  (5)
  • Fibrinogen  (1)
  • 1
    Electronic Resource
    Electronic Resource
    Secretion of hementin and other antihaemostatic factors in the salivary gland complex of the giant amazon leech Haementeria ghilianii (1991)
    Springer
    Comparative clinical pathology 1 (1991), S. 35-41 
    Details
    ISSN: 1433-2981
    Keywords: Hementin ; Antihaemostatic factors ; Salivary gland complex ; Giant Amazon leech ; Fibrinogen ; Fibrinogenolysis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Biological observations were made on the antihaemostatic activity in the saliva of the giant Amazon leech Haementeria ghilianii. Particular emphasis was placed on determining where the fibrino(geno)lytic enzyme hementin is produced and secreted in the salivary gland complex. Hungry third-fed Amazon leeches produce about 650 units of hementin, with by far the majority of the activity (75%) in the two posterior glands. The two anterior glands contain much less hementin (12%), and a small amount (12%) resides in the proboscis itself, presumably in the salivary gland ductules. In the anterior gland, hementin appears to be produced by only certain cells. The secretion of hementin is confined to the lumen of the proboscis. Secretions in the proboscis lumen are rich in antihaemostatic activity, as evidenced by fibrinogenolysis (hementin), prolongation of prothrombin time (PT), activated partial thromboplastin time (APTT), thrombin clotting time (TCT) and Atroxin clotting time, and inhibition of collagen-induced platelet aggregation. In contrast, no anti-haemostatic, including hementin, activity was detectable at the tip. Suprisingly, the wound from the bite by the Amazon leech is not associated with prolonged bleeding. This is in marked contrast to the wound by the European medicinal leech Hirudo medicinalis which bleeds for an average of ten hours. The absence of bleeding is compatible with the interpretation, based on the above findings, that during feeding the Amazon leech does not inject antihaemostatic factors into the host, or at least not in the vicinity of the wound.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00422691
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  • 2
    Electronic Resource
    Electronic Resource
    A novel hollow-fiber reactor with reversible immobilization of lactase (1988)
    Hoboken, NJ : Wiley-Blackwell
    AIChE Journal 34 (1988), S. 293-304 
    Details
    ISSN: 0001-1541
    Keywords: Chemistry ; Chemical Engineering
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Experimental and theoretical studies on a backflush hollow-fiber enzymatic reactor (HFER) were conducted in this work for a lactose/lactase system. An A. niger lactase was chosen, from the four lactases tested, for reversible immobilization in the sponge layers of the fibers. An enzyme loading procedure was developed that allowed reliable and reproducible operation of the hollow-fiber reactor and produced industrially significant conversions without apparent change in the activity or stability of the lactase used. This reversible immobilization scheme also permitted easy replacement of the enzyme used. The performance of the backflush HFER was investigated and a large number of data concerning its operation were obtained and interpreted. Momentum and mass transports in such a HFER were analyzed, and mathematical models that took the experimental findings into consideration were also developed and solved analytically and/or numerically. Predictions from the computer model developed in this work were found to be in excellent agreement with the experimental data collected, suggesting the possibility of a priori design of a process-scale backflush HFER. With minor modifications, the models developed are expected to be applicable to hollow-fiber reactors with a wide selection of immobilized cells, organelles, and other enzymes.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/aic.690340213
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  • 3
    Electronic Resource
    Electronic Resource
    Fast atom bombardment and collisional activation mass spectrometry of retinyl phosphate mannose synthesized by liver membranes (1985)
    Chichester : Wiley-Blackwell
    Biological Mass Spectrometry 12 (1985), S. 221-227 
    Details
    ISSN: 1052-9306
    Keywords: Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Fast atom bombardment (FAB) and collisional activation dissociation (CAD) mass-analysed ion kinetic energy (MIKE) spectra have confirmed the structures of retinyl phosphate (Ret-P), retinyl phosphate mannose (Ret-P-Man) and guanosine 5′-diphospho-D-mannose (GDP-Man). Ret-P-Man was made in vitro while Ret-P and GDP-Man were chemically synthesized. Positive ion FAB mass spectrometry of Ret-P showed an observable short-lived spectrum with a mass ion at m/z 367 [M + H]+, and a major fragment ion at m/z 269 [M+H—H3PO4]+. Negative ion FAB mass spectrometry of Ret-P showed a strong stable spectrum with a parent ion at m/z 365 [M—H]-, a glycerol (G) adduct ion at m/z 457 [M—H+G]- and a dimer ion at m/z 731 [2M—H]-. GDP-Man showed an intense spectrum with parent ion at m/z 604 [M—H]- and cationized species at m/z 626 [M+Na-2H]- and 648 [M+2Na-3H]-. Negative ion FAB mass spectrometry of Ret-P-Man showed a parent ion at m/z 527 [M—H]- and a fragment ion at m/z 259 [C6H12PO9]-. The CAD-MIKE spectra showed structurally significant fragment ions at m/z 442 and 361 for the [M—H]- ion of GDP-Man, and at m/z 509, 406, 364 and 241 for the [M—H]- ion of Ret-P-Man. FAB and CAD-MIKE spectra have been applied successfully to confirm the structure of Ret-P-Man made in vitro from Ret-P and GDP-Man.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bms.1200120507
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  • 4
    Electronic Resource
    Electronic Resource
    Recombinant human secretory phospholipase A2: Purification and characterization of the enzyme for active site studies (1992)
    Chicester [u.a.] : Wiley-Blackwell
    Journal of Molecular Recognition 5 (1992), S. 145-153 
    Details
    ISSN: 0952-3499
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: A secreted form of phospholipase A2 (PLA2) is thought to play an important role in inflammatory diseases. To characterize this enzyme the cDNA encoding a low molecular weight PLA2 was cloned from a human placental cDNA library. The cDNA encoding the human PLA2 was subcloned into an expression vector and subsequently transfected into Chinese hamster ovary (CHO) cells. A stable CHO cell clone, secreting ca I mg/L of recombinant PLA2 into the medium, was scaled up in culture to 180L. The recombinant enzyme was purified from the cell supernatant to apparent homogeneity by a novel procedure combining adsorption to poly(vinylidene difluoride) membranes, ion exchange chromatography and size exclusion chromatography. The final recovery of PLA2 activity was 58%. A direct comparison between the purified recombinant human PLA2 and PLA2 purified from human synovial fluid, including molecular weight, antigenicity, ionic dependence, substrate specificity and sensitivity to know PLA2 inhibitors, indicated that the two enzymes exhibit identical biochemical properties. These results show that the recombinant PLA2 can be efficiently expressed and purified in sufficient quantities to characterize the enzyme active site, to aid in the rational development of PLA2 inhibitors as potential anti-inflammatory drugs, and to investigate further the role of PLA2 in inflammatory disease.
    Additional Material: 8 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jmr.300050405
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  • 5
    Electronic Resource
    Electronic Resource
    Novel poly(n-butyl methacrylate)/titanium oxide alloys produced by te sol-gel process for titanium alkoxides (1990)
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Applied Polymer Science 40 (1990), S. 1401-1420 
    Details
    ISSN: 0021-8995
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology , Mechanical Engineering, Materials Science, Production Engineering, Mining and Metallurgy, Traffic Engineering, Precision Mechanics , Physics
    Notes: A method has been developed to cast novel organic/inorganic hybrid films from multicomponent solutions containing titanium alkoxides, poly(n-butyl methacrylate), water, and isopropanol of prescribed compositions. The sol-gel reactions and controlled drying procedure yielded materials of mechanical integrity for which the multistep thermal degradation profile of the organic polymer has been significantly modified. A crystallization exotherm, presumably due to anatase formation, is seen for tetraethyl titanate-derived films beyond the organic degradation temperature. The trend of mechanical tensile parameters with increasing Ti oxide content depicts progressive material strengthening. FT-IR as well as the thermal and mechanical studies of these films suggest a highly unconnected and heterogeneous Ti oxide phase.
    Additional Material: 14 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/app.1990.070400726
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  • 6
    Electronic Resource
    Electronic Resource
    Glycoconjugates: composition, structure, and function. Edited by Howard J. Allen & Edward C. Kisailus, Marcel Dekker, New York, 1992, vii + 685 pp., price: $195. ISBN 0 8247 8431 6 (1994)
    Chichester : Wiley-Blackwell
    Journal of Chemical Technology AND Biotechnology 59 (1994), S. 115-115 
    Details
    ISSN: 0268-2575
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jctb.280590131
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