Nella presente ricerca sono state studiate le proteine solubili della lente di adulti di Rana esculenta mediante cromatografia a scambio ionico su colonna, elettroforesi su gel di poliacrilamide ed analisi immunoelettroforetica. La cromatografia su colonna delle proteine totali della lente, effettuata con il sistema tampone $NaH_{2}PO_{4}-Na_{2}HPO_{4}-NaCl$, ha rivelato la presenza di sei frazioni. La prima frazione eluita corrisponde alle $\gamma$ cristalline, e rappresenta la frazione predominante; seguono, in ordine di abbondanza, la frazione $\beta$ e la frazione ©. Una ulteriore cromatografia della frazione $\gamma$, isolata e concentrata, ha rivelato la presenza di sei distinte componenti, la cui presenza è confermata dall'analisi elettroforetica su gel di poliacrilamide. L'analisi immunoelettroforetica delle proteine totali ha evidenziato un quadro complesso con la presenza di una componente minore che può essere identificata come una frazione pre-$\alpha$.
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Con il contributo del Ministero per i Beni e le Attività Culturali