Primary sequence dependence of the deamidation of rabbit muscle aldolase

Science. 1974 Jan 11;183(4120):85. doi: 10.1126/science.183.4120.85.

Abstract

The first-order deamidation half-time of the peptide, Gly-Ser-Asn-His-Gly in phosphate butler, pH 7.4, ionic strength at 0.2, 37.0 degrees C, is 6.4 +/- 0.5 days. This compares favorably with the in vivo deamidation half-time of 8 days for this sequence in rabbit muscle aldolase. This fact is discussed with respect to the general hypothesis that sequence-controlled deamidation of glutaminyl and asparaginylresidues is a mechanism by which molecular and organismic development and aging are timed.

MeSH terms

  • Amides
  • Amino Acid Sequence
  • Animals
  • Buffers
  • Carbon Radioisotopes
  • Chemical Phenomena
  • Chemistry
  • Fructose-Bisphosphate Aldolase / metabolism*
  • Hydrogen-Ion Concentration
  • In Vitro Techniques
  • Kinetics
  • Peptides
  • Phosphates
  • Rabbits

Substances

  • Amides
  • Buffers
  • Carbon Radioisotopes
  • Peptides
  • Phosphates
  • Fructose-Bisphosphate Aldolase