Abstract β-Aspartyl peptidase from Escherichia coli has been purified 110-fold in a four-step procedure. Its molecular weight is estimated at 120,000 by gel filtration. The peptidase appears to be specific for β-aspartyl dipeptides, with maximum activity for β-l-aspartyl-l-leucine. The pH optimum is 7.5, but reactions were carried out at pH 8.0 because stability is even greater at the higher pH. The peptidase does not require metal ions for activation and is not a sulfhydryl enzyme. The apparent Km is 8.1 x 10-4 m for β-aspartylleucine.
No takes yet. Share an insight, caveat, or question.
Edward E. Haley (1968) studied this question.
Synapse has enriched 5 closely related papers on similar clinical questions. Consider them for comparative context: