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Activation of pepsin (EC 3.4.4.1) by heavy-metal ions including a contribution to the mode of action of copper sulphate in pig nutrition

Published online by Cambridge University Press:  09 March 2007

M. Kirchgessner ,
M. G. Beyer  and
H. Steinhart
M. Kirchgessner
Affiliation:
Institut für Tierernährung der Technischen Universität München, D-8050 Freising-Weihenstephan, West Germany
M. G. Beyer
Affiliation:
Institut für Tierernährung der Technischen Universität München, D-8050 Freising-Weihenstephan, West Germany
H. Steinhart
Affiliation:
Institut für Tierernährung der Technischen Universität München, D-8050 Freising-Weihenstephan, West Germany
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Abstract

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1. Kinetic experiments were done with pepsin (EC 3.4.4.1) using haemoglobin as a substrate in the presence of different metal cations.

2. The activation of peptic hydrolysis with higher concentrations of cupric ions added to the reaction mixture was determined from turnover-rate curves in experiments with constant substrate concentration. With a Cu2+ concentration greater than 1.67 × 10-4M activation was obtained

3. Nickel ions at a concentration of 8.33 × 10-4 M and at higher concentrations also increased pepsin activity. Additions of ferrous ions and zinc ions had no effect.

4. Experiments were done using variable substrate concentrations in the presence of different Cu2+ concentrations. The concentrations of haemoglobin ([S]) at half maximum velocity were determined. The double-reciprocal plots of [S] v. reaction velocity (v) (i.e. I/[S] v. I/v) had no common intersection point. Therefore the kinetics did not correspond to any of the known kinetics. The activation brought about by Cu2+ cannot easily be explained by the study of the kinetics. Certain simple explanations of the phenomenon can be eliminated.

Type
Papers on General Nutrition
Information
British Journal of Nutrition , Volume 36 , Issue 1 , July 1976 , pp. 15 - 22
Copyright
Copyright © The Nutrition Society 1976

References

Baker, L. E. (1954). J. biol. Chem. 211, 701.CrossRefGoogle Scholar
Beames, R. M. & Lloyd, L. E. (1964). J. Anim. Sci. 23, 1206.Google Scholar
Beyer, M. G., Kirchgessner, M. & Steinhart, H. (1975 a). Z. Tierphysiol. Tierernähr. Futtermittelk. 35, 329.CrossRefGoogle Scholar
Beyer, M. G., Kirchgessner, M. & Steinhart, H. (1975 b). Landw. Forsch. 28, 278.Google Scholar
Beyer, M. G., Steinhart, H. & Kirchgessner, M. (1976). Landw. Forsch. 29, 53.Google Scholar
Braude, R. (1965). Cuprum pro Vita. Trans. Symp. Copper Dev. Ass., Lond. p. 55.Google Scholar
Braude, R. (1967). Wld Rev. Anim. Prod. 3, 69.Google Scholar
Casey, E. J. & Laidler, K. J. (1950). J. Am. chem. Soc. 72, 2159.CrossRefGoogle Scholar
Castell, A. G. & Bowland, J. P. (1968 a). Can. J. Anim. Sci. 48, 403.CrossRefGoogle Scholar
Castell, A. G. & Bowland, J. P. (1968 b). Can. J. Anim. Sci. 48, 415.CrossRefGoogle Scholar
Combs, G. E., Ammerman, C. B., Shirley, R. L. & Wallace, H. D. (1966). J. Anim. Sci. 25, 613.CrossRefGoogle Scholar
Determann, H., Jaworek, D., Kotitschke, R. & Walch, A. (1969). Hoppe-Seyler's Z. physiol. Chem. 350, 379.CrossRefGoogle Scholar
Dixon, M. & Webb, E. C. (1966). Enzymes, 2nd ed., p. 61. London: Longmans, Green & Co. Ltd.Google Scholar
Farries, E. & Angelowa, L. (1967). Landw. Forsch. 20, 137.Google Scholar
Galik, R. (1969). Nutr. Abstr. Rev. 40, 1081.Google Scholar
Hennrich, N. & Brümmer, W. (1973). Pharm. Ind., Berl. 35, 269.Google Scholar
Irving, H. & Williams, R. J. P. (1953). J. chem. Soc. 111, 3192.CrossRefGoogle Scholar
Jackson, W. T., Schlamowitz, M. & Shaw, A. (1965). Biochemistry, Easton 4, 1537.CrossRefGoogle Scholar
Kirchgessner, M. & Giessler, H. (1961). Z. Tierphysiol. Tierernähr. Futtermittelk. 16, 297.CrossRefGoogle Scholar
Kirchgessner, M., Roth, F. X. & Roth-Maier, D. A. (1974). Landw. Forsch. 27, 182.Google Scholar
Kirchgessner, M., Roth-Maier, D. A. & Roth, F. X. (1975). Züchtungskunde 47, 96.Google Scholar
Koshland, D. E., Nemethy, G. & Filmer, D. (1966). Biochemistry, Easton 5, 365.CrossRefGoogle Scholar
Meyer, H. & Kröger, H. (1973). Übers. Tierernähr. 1, 9.Google Scholar
Rick, W. & Fritsch, W.-P. (1970). In Methoden der Enzymatischen Analyse, 2nd ed., p. 362 [Bergmeyer, H. U. editor]. Weinheim: Verlag Chemie.Google Scholar
Schröder, J. (1966). Nahrung 37, 541.CrossRefGoogle Scholar
Steinhart, H., Beyer, M. G. & Kirchgessner, M. (1975). Z. Lebensmittelunters. u.-Forsch. 159, 73.CrossRefGoogle Scholar
Wallace, H. D. (1967). High Level Copper in Swine Feeding. New York: International Copper Research Association Inc.Google Scholar
Young, L. G., Brown, R. G., Ashton, G. C. & Smith, G. C. (1970). Can. J. Anim. Sci. 50, 717.CrossRefGoogle Scholar