Hostname: page-component-78c5997874-dh8gc Total loading time: 0 Render date: 2024-11-18T06:47:59.168Z Has data issue: false hasContentIssue false
  • English
  • Français

An electron microscope study of the ultrastructure of bovine and human casein micelles in fresh and acidified milk

Published online by Cambridge University Press:  01 June 2009

G. G. Calapaj
G. G. Calapaj
Affiliation:
Electron Microscopical Centre of the University of Padua, Italy
Get access Rights & Permissions [Opens in a new window]

Summary

When examined under the electron microscope, bovine casein micelles were seen as aggregates of spheroidal granules arranged in spherical symmetry. The granules were of 2 kinds—one transparent in the electron beam and the other relatively opaque. With increasing acidity of the milk the regular arrangements of granules tended to break down, and bridges composed of granules, formed between neighbouring micelles. The average diameter of the granules was about 8 mμ, from which a molecular weight of about 225000 was calculated. Evidence was adduced for the identity of these granules with the macromolecules of native casein in equilibrium with whey.

Human casein micelles showed the same structural features. The average diameter of the granules was about 6 mμ, from which a molecular weight of about 100000 was calculated.

Type
Original Articles
Information
Journal of Dairy Research , Volume 35 , Issue 1 , February 1968 , pp. 1 - 6
Copyright
Copyright © Proprietors of Journal of Dairy Research 1968

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)

References

REFERENCES

Baud, C. A., Morand, J. C. & Pernoux, E. (1951). C. r. hebd. Séanc. Acad. Sci., Paris 223, 276.Google Scholar
Beeby, R. (1963). J. Dairy Res. 30, 77.CrossRefGoogle Scholar
Birbeck, M. S. C. (1961). Laboratory Manual of Analytical Methods of Protein Chemistry, vol. 3 chap. 1, (ed. Alexander, P. and Block, R. J.). London: Pergamon Press.Google Scholar
Brenner, S. & Horne, R. W. (1959). Biochim. biophys. Acta 34, 103.Google Scholar
Calapaj, G. G. (1962). Boll. 1st. sier. oter milan. 41, 276.Google Scholar
Calapaj, G. G. (1966). Atti V° Congr. ital. Micr. elettr. p. 23 (ed. Soc. It. M.E.). Milano.Google Scholar
D'Agostino Barbaro, A. & Calapaj, G. G. (1958). Acta med. vet., Napoli 4, 9.Google Scholar
Ford, T. F. & Ramsdell, G. A. (1949). 12th Int. Dairy Congr. Stockholm. 2, 17.Google Scholar
Hankinson, C. L. & Briggs, D. R. (1941). J. phys. chem. Ithaca 45, 943.Google Scholar
Hostettler, H. & Imhof, K. (1951). Milchwissenschaft 6, 351, and 400.Google Scholar
Hostettler, H. & Imhof, K. (1952). Landw. Jb. Schweiz 66, 307.Google Scholar
Huth, E. (1957). Mochr. Kinderheilk. 105, 247.Google Scholar
Knoop, E. & Wortmann, A. (1960). Milchwissenschaft 15, 273.Google Scholar
Nichols, J. E., Bailey, E. D., Hahn, G. E., Greenbank, G. R. & Deysher, E. F. (1931). J. phys. Chem. Ithaca 35, 1303.Google Scholar
Nitschmann, H. (1949). Helv. chim. Acta 32, 1258.Google Scholar
Shimmin, P. D. & Hill, R. D. (1964). J. Dairy Res. 31, 121.Google Scholar
Svedberg, T., Carpenter, L. M. & Carpenter, G. (1930). J. Am. chem. Soc. 52, 241.Google Scholar
Waugh, D. F. & Von Hippel, P. H. (1956). J. Am. chem. Soc. 78, 4576.Google Scholar