Identification of the apparently essential lysine residues in phospholipase C (Bacillus cereus)
Phospholipase C (Bacillus cereus) contains two apparently essential and very reactive lysine residues that may be labelled selectively by pyridoxal 5'-phosphate [Aurebekk & Little (1977) Biochem, J. 161, 159--165]. One of these lysine residues was found in the 25-amino acid N-terminal fragm...
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Veröffentlicht in: | Biochemical journal 1981-03, Vol.193 (3), p.805-809 |
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Format: | Artikel |
Sprache: | eng |
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Zusammenfassung: | Phospholipase C (Bacillus cereus) contains two apparently essential and very reactive lysine residues that may be labelled selectively by pyridoxal 5'-phosphate [Aurebekk & Little (1977) Biochem, J. 161, 159--165]. One of these lysine residues was found in the 25-amino acid N-terminal fragment liberated by CNBr digestion of the pyridoxal-labelled enzyme and identified as lysine-6. Two of the labelled peptides isolated from the chymotryptic digest of pyridoxal-labelled enzyme contained proline, suggesting that the other labelled lysine residue is situated in the same region of the primary structure as the single proline residue of the enzyme. |
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ISSN: | 0264-6021 1470-8728 |
DOI: | 10.1042/bj1930805 |