S-aminopropylcysteine and S-aminoethylhomocysteine are oxidized by snake venom L-amino acid oxidase in the presence of catalase with formation of the respective ketoderivatives. Only the ketoderivative of S-aminopropylcysteine cyclizes to give a seven membered ring (ketimine) absorbing at 296 nm. In the absence of catalase both ketoderivatives are oxidatively decarboxylated.
OXIDATIVE DEAMINATION OF S-AMINOPROPYLCYSTEINE AND S-AMINOETHYLHOMOCYSTEINE / I., Serao; Costa, Mara; Pecci, Laura; Coccia, Raffaella; Cavallini, Doriano. - In: ITALIAN JOURNAL OF BIOCHEMISTRY. - ISSN 0021-2938. - STAMPA. - 40:(1991), pp. 216-222.
OXIDATIVE DEAMINATION OF S-AMINOPROPYLCYSTEINE AND S-AMINOETHYLHOMOCYSTEINE
COSTA, Mara;PECCI, Laura;COCCIA, Raffaella;CAVALLINI, Doriano
1991
Abstract
S-aminopropylcysteine and S-aminoethylhomocysteine are oxidized by snake venom L-amino acid oxidase in the presence of catalase with formation of the respective ketoderivatives. Only the ketoderivative of S-aminopropylcysteine cyclizes to give a seven membered ring (ketimine) absorbing at 296 nm. In the absence of catalase both ketoderivatives are oxidatively decarboxylated.File allegati a questo prodotto
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