Abstract
κ-Casein has been reduced by LiBH4. A precipitate (P) and a supernatant (S) containing a substance soluble in 12% trichloroacetic acid and not dialysable are obtained: they seem to be very closely related respectively to para-κ-casein and κ-caseino-glycopeptide both obtained after rennin-digestion of κ-casein. Phenylalanine is the C-terminal amino acid of para-κ-casein and phenylalaninol has been detected in the precipitate (P). LiBH4 reduces the rennin-sensitive linkage in κ-casein which seems to be an ester linkage involving the carboxyl group of the C-terminal phenylalanine residue of para-κ-casein.
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