Characterization of papaya peptidase A as an enzyme of extreme basicity.
Papaya peptidase A, a papain-like enzyme, has formerly been shown to contain a larger excess of basic amino acids and to have 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 now 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.
D003546:Cysteine Endopeptidases; D010450:Endopeptidases / Q000302:isolation & purification* / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D010206:Papain / Q000302:isolation & purification / Q000378:metabolism; D010940:Plant Proteins; D010944:Plants / Q000201:enzymology*
D010940:Plant Proteins; D010450:Endopeptidases; D003546:Cysteine Endopeptidases; D010206:Papain; C039974:caricain