Skip to main content
NCBI home page
Biochemical Journal logoLink to Biochemical Journal
. 1983 Aug 1;213(2):559–560. doi: 10.1042/bj2130559

A re-evaluation of the nomenclature of the cysteine proteinases of Carica papaya and a rational basis for their identification.

K Brocklehurst, E Salih
PMCID: PMC1152164  PMID: 6351846

Full text

PDF
559

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Asbóth B., Polgár L. Transition-state stabilization at the oxyanion binding sites of serine and thiol proteinases: hydrolyses of thiono and oxygen esters. Biochemistry. 1983 Jan 4;22(1):117–122. doi: 10.1021/bi00270a017. [DOI] [PubMed] [Google Scholar]
  2. Baines B. S., Brocklehurst K. Characterization of papaya peptidase A as a cysteine proteinase of Carica papaya L. with active-centre properties that differ from those of papain by using 2,2'-dipyridyl disulphide and 4-chloro-7-nitrobenzofurazan as reactivity probes. Use of two-protonic-state electrophiles in the identification of catalytic-site thiol groups. Biochem J. 1982 Jul 1;205(1):205–211. doi: 10.1042/bj2050205. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Balls A. K., Lineweaver H., Thompson R. R. CRYSTALLINE PAPAIN. Science. 1937 Oct 22;86(2234):379–379. doi: 10.1126/science.86.2234.379. [DOI] [PubMed] [Google Scholar]
  4. Brocklehurst K., Baines B. S., Mushiri M. S. Evidence that the active centre of chymopapain A is different from the active centres of some other cysteine proteinases and that the Brønsted coefficient (beta nuc.) for the reactions of thiolate anions with 2,2'-dipyridyl disulphide may be decreased by reagent protonation. Biochem J. 1980 Jul 1;189(1):189–129. doi: 10.1042/bj1890189. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Brocklehurst K. Two-protonic-state electrophiles as probes of enzyme mechanisms. Methods Enzymol. 1982;87:427–469. doi: 10.1016/s0076-6879(82)87026-2. [DOI] [PubMed] [Google Scholar]
  6. Clagett J. A., Tokuda S., Engelhard W. E. Chymopapain C, an immunosuppressive protease. I. Partial purification and characterization. Proc Soc Exp Biol Med. 1974 Apr;145(4):1250–1257. doi: 10.3181/00379727-145-37991. [DOI] [PubMed] [Google Scholar]
  7. EBATA M., YASUNOBU K. T. Chymopapain. I. Isolation, crystallization, and preliminary characterization. J Biol Chem. 1962 Apr;237:1086–1094. [PubMed] [Google Scholar]
  8. Joshi P. N., Shankar V., Abraham K. I., Sreenivasan K. Separation of chymopapain from papaya latex (Carica papaya) on amberlite IR-120 (Hg2+). J Chromatogr. 1976 Jun 9;121(1):65–71. doi: 10.1016/s0021-9673(00)82298-0. [DOI] [PubMed] [Google Scholar]
  9. KIMMEL J. R., SMITH E. L. Crystalline papain. I. Preparation, specificity, and activation. J Biol Chem. 1954 Apr;207(2):515–531. [PubMed] [Google Scholar]
  10. Kunimitsu D. K., Yasunobu K. T. Chymopapain. IV. The chromatographic fractionation of partially purified chymopapain and the characterization of crystalline chymopapain B. Biochim Biophys Acta. 1967 Jul 11;139(2):405–417. doi: 10.1016/0005-2744(67)90044-7. [DOI] [PubMed] [Google Scholar]
  11. Lynn K. R. A purification and some properties of two proteases from papaya latex. Biochim Biophys Acta. 1979 Aug 15;569(2):193–201. doi: 10.1016/0005-2744(79)90054-8. [DOI] [PubMed] [Google Scholar]
  12. Lynn K. R. An isolation of chymopapain. J Chromatogr. 1973 Sep 26;84(2):423–425. doi: 10.1016/s0021-9673(01)91729-7. [DOI] [PubMed] [Google Scholar]
  13. Polgár L. Isolation of highly active papaya peptidases A and B from commercial chymopapain. Biochim Biophys Acta. 1981 Apr 14;658(2):262–269. doi: 10.1016/0005-2744(81)90296-5. [DOI] [PubMed] [Google Scholar]
  14. Robinson G. W. Isolation and characterization of papaya peptidase A from commercial chymopapain. Biochemistry. 1975 Aug 12;14(16):3695–3700. doi: 10.1021/bi00687a028. [DOI] [PubMed] [Google Scholar]
  15. Schack P. Fractionation of proteolytic enzymes of dried papaya latex. Isolation and preliminary characterization of a new proteolytic enzyme. C R Trav Lab Carlsberg. 1967;36(4):67–83. [PubMed] [Google Scholar]

Articles from Biochemical Journal are provided here courtesy of The Biochemical Society

RESOURCES