Search Reference

3.4.22.25

Isolation of highly active papaya peptidases A and B from commercial chymopapain

Biochim. Biophys. Acta

658

262-269

1981

3.4.22.25

Chromatographic and electrophoretic analyses of papaya proteinases

Phytochemistry

26

75-79

1987

-

3.4.22.25

Affinity purification of the novel cysteine proteinase papaya proteinase IV, and papain from papaya latex

Biochem. J.

261

469-476

1989

3.4.22.25

Papaya proteinase IV amino acid sequence

FEBS Lett.

258

109-112

1989

3.4.22.25

Interactions of papaya proteinase IV with inhibitors

FEBS Lett.

262

58-60

1990

3.4.22.25

Selective cleavage of glycyl bonds by papaya proteinase IV

FEBS Lett.

260

195-197

1990

3.4.22.25

Three-dimensional structure and thiol reactivity characteristics of chymopapain M (papaya proteinase IV)

Biochem. Soc. Trans.

18

934-935

1990

3.4.22.25

Factors effecting the thermostability of cysteine proteinases from Carica papaya

Eur. J. Biochem.

214

129-134

1993

3.4.22.25

Glycyl endopeptidase

Methods Enzymol.

244

539-555

1994

3.4.22.25

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

Biochem. J.

300

805-820

1994