Hostname: page-component-586b7cd67f-l7hp2 Total loading time: 0 Render date: 2024-11-29T02:57:54.392Z Has data issue: false hasContentIssue false
  • English
  • Français

Mechanisms of heat damage in proteins

1. Models with acylated lysine units*

Published online by Cambridge University Press:  09 March 2007

J. Bjarnson  and
K. J. Carpenter
J. Bjarnson
Affiliation:
School of Agriculture, University of Cambridge
K. J. Carpenter
Affiliation:
School of Agriculture, University of Cambridge
Rights & Permissions [Opens in a new window]

Abstract

Core share and HTML view are not available for this content. However, as you have access to this content, a full PDF is available via the ‘Save PDF’ action button.

1. ě-N-Acetyl-L-lysine showed a growth-promoting value for the young rat receiving a lysine-deficient diet approximately half that of the equivalent quantity of L-lysine; ě-N-propionyl-L-lysine showed negligible activity.

2. Considerable quantities of lysine were recovered from acid-hydrolysis of the urine of rats receiving these two compounds. Qualitative chromatography suggested that the compounds themselves were appearing in the urine.

3. Similar results were obtained from giving proteins that had the ě-NH2, groups of their lysine units either acetylated or propionylated.

4. Giving a pure protein in which the nutritional availability of the lysine had been reduced heat treatment resulted in greatly increased faecal lysine but little urinary lysine.

Type
Research Article
Information
British Journal of Nutrition , Volume 23 , Issue 4 , November 1969 , pp. 859 - 868
Copyright
Copyright © The Nutrition Society 1969

References

Association of Official Agricultural Chemists (1965). Official Methods of Analysis, 10th ed.Washington, DC: Association of Official Agricultural Chemists.Google Scholar
Bjarnason, J. & Carpenter, K. J. (1969). Proc. Nutr. Soc. 28, 2A.Google Scholar
Carpenter, K. J. (1957). Proc. int. Congr. Nutr. IV. Paris. Abstr. Pap. p. 154.Google Scholar
Carpenter, K. J. (1960). Biochem. J. 77, 604.CrossRefGoogle Scholar
Carpenter, K. J., Morgan, C. B., Lea, C. H. & Parr, L. J. (1962). Br. J. Nutr. 16, 451.CrossRefGoogle Scholar
Chapman, D. G., Castillo, R. & Campbell, J. A. (1959). Can. J. Biochem. Physiol. 37, 679.CrossRefGoogle Scholar
Fraenkel-Conrat, H., Bean, R. S. & Lineweaver, H. (1949). J. biol. Chem. 177, 385.CrossRefGoogle Scholar
Hendrix, B. M. & Paquin, F. Jr (1938). J. biol. Chem. 124, 135.CrossRefGoogle Scholar
Hill, R. L. (1965). Adv. Protein Chem. 20, 37.CrossRefGoogle Scholar
Lane-Petter, W., Lane-Petter, M. E. & Bowtell, C. W. (1968). Lab. Anim. 2, 35.CrossRefGoogle Scholar
Leclerc, J. & Benoiton, L. (1968 a). Can. J. Biochem. 46, 471.CrossRefGoogle Scholar
Leclerc, J. & Benoiton, L. (1968 b). Can. J. Chem. 46, 1047.CrossRefGoogle Scholar
Ma, T. S. & Zuazaga, G. (1942). Ind. Engng Chem. analyt. Edn 14, 280.CrossRefGoogle Scholar
Neuberger, A. & Sanger, F. (1943). Biochem. J. 37, 515.CrossRefGoogle Scholar
Olcott, H. S. & Fraenkel-Conrat, H. (1947). Chem. Rev. 41, 151.CrossRefGoogle Scholar
Paik, W. K. & Benoiton, L. (1963). Can. J. Biochem. Physiol. 41, 1643.CrossRefGoogle Scholar
Rao, S. R., Carter, F. L. & Frampton, V. L. (1963). Analyt. Chem. 35, 1927.CrossRefGoogle Scholar
Roach, A. G., Sanderson, P. & Williams, D. R. (1967). J. Sci. Fd Agric. 18, 274.CrossRefGoogle Scholar
Tazawa, Y. (1943). Acta Phytochim. 13, 177.Google Scholar
Vratsanos, S. M. (1960). Archs Biochem. Biophys. 90, 132.CrossRefGoogle Scholar