Interactions of papaya proteinase IV with inhibitors
Isolation of highly active papaya peptidases A and B from commercial chymopapain
Biochim. Biophys. Acta
Kinetic constants for the hydrolysis of aggrecan by the papaya proteinases and their relevance for chemonucleolysis
Arch. Biochem. Biophys.
Papaya proteinase IV amino acid sequence
Selective cleavage of glycyl bonds by papaya proteinase IV
Solid-to-solid peptide synthesis by glycyl endopeptidase
Enzyme Microb. Technol.
Structural characterization of the papaya cysteine proteinases at low pH
Biochem. Biophys. Res. Commun.
Structure of chymopapain M the late-eluted chymopapain deduced by comparative modelling techniques and active-centre characteristics determined by pH-dependent kinetics of catalysis and reactions with time-dependent inhibitors: the Cys-25/His-159 ion-pair is insufficient for catalytic competence in both chymopapain M and papain
The proregion of papaya proteinase IV inhibits Colorado potato beetle digestive cysteine proteinases
The structural origins of the unusual specificities observed in the isolation of chymopapain M and actinidin by covalent chromatography and the lack of inhibition of chymopapain M by cystatin