Über Die in Organischen Persäuren Löslichen Proteine Der Wolle Unter Besonderer Berücksichtigung Der Tyrosinreichen Proteine
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Die erste Sequenzermittlung eines Proteins, des Insulins, durch Sanger (1) 1955 zeigt die wesentlichen Schritte fUr die StrukturaufkHirung eines Disul- fidproteins, namlich die se1ektive Spaltung der Cystinbrucken, Trennung und Reinigung der entstehenden Fraktionen und schlieinich die Charakteri- sierung der einheitlichen Peptide. Auch bei der chemischen Untersuchung der Wolle, die ein besonders kompliziertes System von Disulfidproteinen darste1lt, hat man versucht, diesen Weg zu gehen. Die klassischen Ver- fahren zur Gewinnung loslicher Proteine aus Wolle unterscheiden sich hauptsachlich in den Methoden, die zur Spaltung der Cystinbrucken ange- wendet werden. Goddard und Michaelis zeigten 1934, daB man Keratin durch Reduktion mit Thiog1ykolat in Losung bringen kann (2). Den Weg zur selektiven Oxydation von Cystin in Proteinen wiesen G. Toennies und R. P. Homiller, die 1942 feststellten, daB Perameisensaure nur Tryptophan, Methionin und Cystin oxydiert (3). Sie fanden, daB z. B. beim Casein, das in Ameisensaure ge- lOst war, nur diese drei Aminosauren mit zugesetztem Wasserstoffperoxid reagierten (4). Alexander und Mitarbeiter ubertrugen diese Erkenntnisse auf die Keratinforschung (5). Sie konnten nachweis en, daB Peressigsaure ahnlich spezifisch wirkt wie Perameisensaure und zudem den Vorteil einer groBeren Stabilitat in waBriger Losung bietet, was bereits D' Ans und Kneip 1915 festgestellt hatten (6). Nach Oxydation mit Peressig- oder Peramei- sensaure werden etwa 90 % des Wollkeratins in verdunntem Ammoniak 10s- lich (7)(8)(9). Durch Ansauern kann man daraus etwa 60 % ausfallen, die sogenannte "a-Keratose", wahrend die" t-Keratose" in Losung bleibt. Der in Sauren und Laugen un10sliche Anteil der oxydierten Wolle wird "/3-Keratose" genannt (10).
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