Springer Online Journal Archives 1860-2000
Abstract InEscherichia coli, NADP+-specific isocitrate dehydrogenase (EC 220.127.116.11) may undergo a phosphorylation catalyzed by a cAMP-independent protein kinase, with a concomitant decrease in catalytic activity. In this report, we describe the purification and amino acid sequence of a32P-labeled peptide obtained from in vivo32P-labeled isocitrate dehydrogenase. The32P-labeled peptide was isolated from a tryptic digest and found to contain seven amino acids, including a single serine residue. Following automated Edman degradation and reversephase high-pressure liquid chromatography of the phenylthiohydantoin-amino acids, the sequence of this peptide was established to be-Ser(P)-Leu-Asn-Val-Ala-Leu-Arg.
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