Die Bildung von Lanthionin- und Lysinoalanin-Querbrücken bei der alkalischen Denaturierung von Rinderserumalbumin

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Abstract
The denaturation of bovine serum albumin was studied, using the usual chemical methods of protein analysis. In buffers containing urea, at pH values between 9. 0 and 12.5 lanthionine and lysinoalanine cross linkages are formed. The denaturation product was separated into 3 fractions by gel filtration on Sephadex G-200; each fraction had a different average molecular weight, but the same lanthionine content. Therefore, the newly formed cross linkages cannot all be formed between different polypeptide chains. The formation of the thio-ether bridges of lanthionine and the methyleneaminobutylene bridges of lysinoalanine cause an irreversible change in conformation; the protein cannot be renatured.