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Serological and fluorescence studies of the heat stability of bovine lactoferrin

Published online by Cambridge University Press:  01 June 2009

Augustin Baer ,
Marko Oroz  and
Bernard Blanc
Augustin Baer
Affiliation:
Federal Dairy Research Institute, CH-3097 Liebefeld (Bern), Switzerland
Marko Oroz
Affiliation:
Federal Dairy Research Institute, CH-3097 Liebefeld (Bern), Switzerland
Bernard Blanc
Affiliation:
Federal Dairy Research Institute, CH-3097 Liebefeld (Bern), Switzerland
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Summary

The heat denaturation of Fe-saturated lactoferrin (If) and Fe-free lactoferrin (apo-lf) was studied using the methods of micro-complement fixation and fluorescence. It was established that the change in conformation of apo-lf, induced by iron binding, conferred a higher heat stability to the molecule: the changes were observed at temperatures above 40 °C for apo-lf and above 60 °C for If. The Fe-binding ability of the protein was partially independent of the degree of denaturation. Fluorescence analyses indicated that tryptophan residues were probably not directly involved in the metal binding. There was no evidence of antibodies interfering with the binding sites.

Type
Original Articles
Information
Journal of Dairy Research , Volume 46 , Issue 1 , January 1979 , pp. 83 - 93
Copyright
Copyright © Proprietors of Journal of Dairy Research 1979

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References

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