Characterization of Papaya Peptidase A as an Enzyme of Extreme Basicity.
- 1 January 1983
- journal article
- research article
- Published by Danish Chemical Society in Acta Chemica Scandinavica
- Vol. 37b (7) , 607-611
- https://doi.org/10.3891/acta.chem.scand.37b-0607
Abstract
Papaya peptidase A, a papain-like enzyme, has a larger excess of basic amino acids and a higher isoelectric point than any of the other enzymes in the papaya latex. Determinations of the free electrophoretic mobility as a function of pH establishes the isoelectric point of papaya peptidase A as 11.7 and that of succinylated papaya peptidase A as 3.8. Although the specific activity of the enzyme appears only slightly affected by the succinylation, the accompanying change in the charge/mobility ratio seems to indicate a relatively large conformational change upon succinylation.This publication has 2 references indexed in Scilit:
- THE REACTION OF ACETYLCHOLINE AND OTHER CARBOXYLIC ACID DERIVATIVES WITH HYDROXYLAMINE, AND ITS ANALYTICAL APPLICATIONPublished by Elsevier ,2021
- Thermodynamic Proton-, Cadmium-, and Zinc-Binding Constants of Serum Albumin Determined by Zone ElectrophoresisJournal of Biological Chemistry, 1960