A hexadecapeptide containing the azomethine lysine residue has been isolated from 2-keto-3-deoxy-6-phosphogluconate aldolase following incubation with 14C-pyruvate and sodium borohydride, carboxymethylation, and digestion of the derivatized aldolase with trypsin. The radioactive peptide was isolated by gel filtration and ion exchange chromatography. The amino acid sequence was established as: Phe-e-N-(1-carboxyethyl)-Lys-Leu-Phe-Pro-Ala-Glu-Ile-Ser-Gly-Gly-Val-Ala-Ala-Ile-Lys This sequence bears no similarity to those of active site peptides of Class I fructose 1,6-diphosphate aldolases from mammalian tissue.
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Robertson et al. (1971) studied this question.
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