Acetylation of the Amino Groups of Carboxypeptidase A*
- 1 November 1962
- journal article
- research article
- Published by Oxford University Press (OUP) in The Journal of Biochemistry
- Vol. 52 (5) , 363-366
- https://doi.org/10.1093/oxfordjournals.jbchem.a127628
Abstract
The enzyme was denatured in 0.6% Brij 35 dissolved in 50% saturated Na acetate for 24 hrs. at 25[degree]C. The unfolded enzyme was incubated with acetic anhydride in the presence of 0.6% Brij 35, which yielded the enzyme acetylated at alpha-NH2 of N-terminal asparagine and less completely (80%) at epsilon-NH2 of lysine residues. The acetylated preparation retained full enzymic activity.Keywords
This publication has 4 references indexed in Scilit:
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- Metallocarboxypeptidases: Stability Constants and Enzymatic CharacteristicsJournal of Biological Chemistry, 1961
- AMINO ACID COMPOSITION OF CRYSTALLINE CARBOXYPEPTIDASEJournal of Biological Chemistry, 1954
- A STUDY OF CONDITIONS FOR KJELDAHL DETERMINATION OF NITROGEN IN PROTEINS - DESCRIPTION OF METHODS WITH MERCURY AS CATALYST, AND TITRIMETRIC AND GASOMETRIC MEASUREMENTS OF THE AMMONIA FORMED1948