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. 1972 Jul;69(7):1816–1819. doi: 10.1073/pnas.69.7.1816

Deamidation In Vivo of an Asparagine Residue of Rabbit Muscle Aldolase

Christian F Midelfort 1, Alan H Mehler 1,*
PMCID: PMC426809  PMID: 4505659

Abstract

Microheterogeneity of rabbit muscle aldolase is caused by deamidation in vivo of an asparagine residue near the C-terminus of each subunit. Isotopic labeling of a peptide containing the asparagine residue at various time intervals before isolation of aldolase permits estimation of the half-time for the deamidation as about 8 days, which is about the time estimated for the half-life of the enzyme in vivo. It is concluded that the aldolase as genetically determined is a tetramer, designated α4, that undergoes random deamidation to form α3β, α2β2, and αβ3 species as intermediates in the formation of β4, the species in which all of the specific asparagine has been deamidated. Isoelectric focusing data indicate that the subunits do not exchange appreciably in vivo.

Keywords: isozymes, electrofocusing, subunits, protein structure

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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