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  • 1
    Electronic Resource
    Electronic Resource
    Effect of aluminum on the binding properties of α-chymotrypsin (1997)
    Springer
    JBIC 2 (1997), S. 320-326 
    Details
    ISSN: 1432-1327
    Keywords: Key words Proteinases ; Aluminum ; Allosteric modulation ; Metal pollution ; Alzheimer's disease
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract  The effect of aluminum ions on the binding properties of α-chymotrypsin has been studied. The results show that aluminum does not affect the catalytic rate constant k cat, but it acts as an enzyme activator favoring the binding of the substrate to the catalytic site (i.e. decreasing K m). Furthermore, aluminum binding to α-chymotrypsin displays about a threefold decrease in its affinity for the macromolecular inhibitor bovine pancreatic trypsin inhibitor (BPTI). Altogether, the different effect of aluminum on the binding of synthetic substrates (e.g. N-α-benzoyl-l-tyrosine ethyl ester, BTEE) and macromolecular inhibitors (e.g. BPTI) to α-chymotrypsin suggests the occurrence of an aluminum-linked conformational change in the enzyme molecule which brings about a marked structural change at the primary and secondary recognition sites for substrates and inhibitors. The modulative effect exerted by aluminum on the enzyme hydrolytic activity has been investigated also as a function of pH. The ion-linked effect appears to be dependent on the pH in a complex fashion, which suggests that aluminum binding is controlled by the protonation of at least two classes of residues on the enzyme molecule.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s007750050138
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  • 2
    Electronic Resource
    Electronic Resource
    Effect of drugs on oxidation and precipitation of the isolated chains of human hemoglobin (1978)
    Springer
    Molecular and cellular biochemistry 19 (1978), S. 43-48 
    Details
    ISSN: 1573-4919
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Summary The paper deals with the action of: primaquine, epinephrine, adrenochrome, acetylphenylhydrazine and sulphanilamide on the autoxidation of the isolated chains from human hemoglobin and on the precipitation which follows. The effect of superoxide dismutase and catalase on the drug induced autoxidation allows the assessment of the possible role of 02 derivatives (notably superoxide or peroxide) in the overall reaction mechanism. It is also shown that primaquine and acetylphenylhydrazine enhance precipitation of the isolated oxidized chains, while epinephrine and adrenochrome display a small inhibitory effect on precipitation. These effects do not involve O2 radicals, but have presumably to be related to a destabilizing (or stabilizing) action of the drugs on the structure of the protein.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00231233
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  • 3
    Electronic Resource
    Electronic Resource
    Interaction between leukocytic elastase and Kunitz-type inhibitors from bovine spleen (1989)
    Springer
    The protein journal 8 (1989), S. 51-60 
    Details
    ISSN: 1573-4943
    Keywords: leukocytic elastase ; BPTI-like inhibitors ; association constants ; hydrophobic interactions
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract The four Kunitz-type protease inhibitors purified from bovine spleen, which include the basic pancreatic trypsin inhibitor (BPTI), form stable complexes with human leukocytic elastase. The values of the affinity constants of these complexes are similar, in agreement with the great structural similarity of the four inhibitors, but are lower than those measured for the complexes with other serine proteases. Two main factors appear to be responsible for the stability of these complexes, i.e., hydrophobic interactions and ionization phenomena that take place during complex formation. These two factors have been analyzed in terms of the general model previously used for describing the interaction between the serine proteases and their natural inhibitors.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01025078
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  • 4
    Electronic Resource
    Electronic Resource
    Binding of basic pancreatic trypsin inhibitor and related isoinhibitors to leukocytic elastase. Determination of thermodynamic parameters (1989)
    Chicester [u.a.] : Wiley-Blackwell
    Journal of Molecular Recognition 2 (1989), S. 142-146 
    Details
    ISSN: 0952-3499
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: The effect of temperature, ionic strength and solvation power of mono- and divalent cations on the interaction of BPTI-like inhibitors with human leukocytic elastase has been determined. The binding process is characterized by a non-linear dependence of the equilibrium association constant on 1/T indicating a thermal transition at temperature values ranging between 20°C and 35°C depending on the solvent. The marked dependence of the thermodynamic parameters (ΔH°, ΔS°, ΔG°) and of the transition temperature on the concentration and nature of the cations present in solution seems to indicate that the transition, probably of conformational nature, is related to removal of water molecules upon enzyme/inhibitor complex formation.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jmr.300020307
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  • 5
    Electronic Resource
    Electronic Resource
    Cellular localization of bovine pancreatic trypsin inhibitor and related molecular forms in bovine lung (1988)
    Springer
    Journal of molecular histology 20 (1988), S. 187-193 
    Details
    ISSN: 1573-6865
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary In addition to bovine pancreatic trypsin inhibitor (BPTI), three BPTI-related molecular forms (isoinhibitors I, II and III) were isolated from bovine lung by affinity chromatography on immobilized trypsin and subsequently purified by Fast Protein Liquid Chromatography. These inhibitors are identical to the isoinhibitors previously isolated from bovine spleen. Their localization in bovine lung was studied by immunohistochemical techniques, using two different immunoglobulin preparations, selectively recognizing BPTI or the other molecular forms. BPTI-related immunoreactivity was found to be restricted to isolated cells, often identified as mast cells by Toluidine Blue staining. In contrast, isoinhibitor-related immunoreactivity, which also occurs in the mast cells, is present in a number of other cell types. These types include: (i) the smooth muscle cells of different calibre vessels, (ii) the ciliated cells of the bronchial epithelium and the related mucus, and (iii) many cells at alveolar level. Comparison of these data with previous results obtained for bovine spleen suggest multiple physiological roles for these inhibitors.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01747462
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  • 6
    Electronic Resource
    Electronic Resource
    Identification and immunohistochemical localization of various bovine pancreatic trypsin inhibitor-isoforms in bovine pituitary gland (1989)
    Springer
    Journal of molecular histology 21 (1989), S. 721-730 
    Details
    ISSN: 1573-6865
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Three isoinhibitors of bovine pancreatic trypsin inhibitor (BPTI) have been identified and isolated from bovine pituitary gland. The results of the purification process by affinity chromatography on immobilized trypsin, the electrophoretic mobility in non-denaturing conditions, the antiproteolytic activity and the immunochemical reactions indicate that these inhibitors correspond to those previously isolated from bovine spleen and lung. In addition, immunohistochemical experiments show that the isoinhibitors and BPTI are exclusively localized in the mast cells, and not in the endocrine cells, of the pars intermedia and posterior lobe (neurohypophysis) of the pituitary gland. The physiological implications of these findings are discussed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01002838
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    Paper (German National Licenses)
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