Primary sequence dependence of the deamidation of rabbit muscle aldolase.
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.
D000577:Amides; D000595:Amino Acid Sequence; D000818:Animals; D002021:Buffers; D002250:Carbon Radioisotopes; D055598:Chemical Phenomena; D002621:Chemistry; D005634:Fructose-Bisphosphate Aldolase / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D066298:In Vitro Techniques; D007700:Kinetics; D010455:Peptides; D010710:Phosphates; D011817:Rabbits
D000577:Amides; D002021:Buffers; D002250:Carbon Radioisotopes; D010455:Peptides; D010710:Phosphates; D005634:Fructose-Bisphosphate Aldolase