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Tryptic hydrolysis of inorcanic pyrophosphate modified by phosphate and O-phosphoethanolamine

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Abstract

By the peptide map method, a phosphorylated peptide has been isolated from a tryptic hydrolysate of phosphorylated yeast inorganic pyrophosphatase (I), and this is a direct proof of the formation of a covalent bond between (I) and phosphate in the course of this reaction. The isolation and analysis of the peptide from the tryptic hydrolysate shows that the phosphate acceptor is probably the aspartic acid residue 240 or 248. Analysis of a tryptic hydrolysate of (I) modified with O-phosphoethanolamine has shown that O-phosphoethanolamine forms an amide bond with the carboxy group of the same aspartic acid residue. In an alkaline medium, the phosphate residue migrates to the imidazole ring of a histidine residue, apparently that present in position 222.

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Authors
  1. N. P. Bakuleva
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  2. A. A. Komissarov
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  3. A. V. Kuznetsov
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  4. T. I. Nazarova
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  5. V. A. Sklyankina
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  6. S. M. Avaeva
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Additional information

M. V. Lomonosov Moscow State University. Translated from Khimiya Prirodnykh Soedinenii, No. 3, pp. 379–384, May–June, 1982.

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Bakuleva, N.P., Komissarov, A.A., Kuznetsov, A.V. et al. Tryptic hydrolysis of inorcanic pyrophosphate modified by phosphate and O-phosphoethanolamine. Chem Nat Compd 18, 350–355 (1982). https://doi.org/10.1007/BF00580466

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  • DOI: https://doi.org/10.1007/BF00580466

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