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. 1964 Oct;52(4):884–889. doi: 10.1073/pnas.52.4.884

TRYPSINOGEN AND CHYMOTRYPSINOGEN AS HOMOLOGOUS PROTEINS

Kenneth A Walsh 1, Hans Neurath 1
PMCID: PMC300366  PMID: 14224394

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Selected References

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

  1. BRAUNITZER G., GEHRING-MUELLER R., HILSCHMANN N., HILSE K., HOBOM G., RUDLOFF V., WITTMANN-LIEBOLD B. [The structure of normal adult human hemoglobins]. Hoppe Seylers Z Physiol Chem. 1961 Sep 20;325:283–286. doi: 10.1515/bchm2.1961.325.1.283. [DOI] [PubMed] [Google Scholar]
  2. CHARLES M., ROVERY M., GUIDONI A., DESNUELLE P. [On pork trypsinogen and trypsin]. Biochim Biophys Acta. 1963 Jan 1;69:115–129. doi: 10.1016/0006-3002(63)91231-9. [DOI] [PubMed] [Google Scholar]
  3. DESNUELLE P., ROVERY M. The proteins of the exocrine pancreas. Adv Protein Chem. 1961;16:139–195. doi: 10.1016/s0065-3233(08)60029-7. [DOI] [PubMed] [Google Scholar]
  4. DIXON G. H., KAUFFMAN D. L., NEURATH H. Amino acid sequence in the region of diisopropylphosphoryl binding in diisopropylphosphoryl-trypsin. J Biol Chem. 1958 Dec;233(6):1373–1381. [PubMed] [Google Scholar]
  5. DIXON G. H., KAUFFMAN D. L., NEURATH H. Amino acid sequence in the region of diisopropylphosphoryl binding in diisopropylphosphoryl-trypsin. J Biol Chem. 1958 Dec;233(6):1373–1381. [PubMed] [Google Scholar]
  6. DIXON G. H., NEURATH H., PECHERE J. F. Proteolytic enzymes. Annu Rev Biochem. 1958;27(3):489–532. doi: 10.1146/annurev.bi.27.070158.002421. [DOI] [PubMed] [Google Scholar]
  7. Gutfreund H., Sturtevant J. M. THE MECHANISM OF CHYMOTRYPSIN-CATALYZED REACTIONS. Proc Natl Acad Sci U S A. 1956 Oct;42(10):719–728. doi: 10.1073/pnas.42.10.719. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. HARTLEY B. S. AMINO-ACID SEQUENCE OF BOVINE CHYMOTRYPSINOGEN-A. Nature. 1964 Mar 28;201:1284–1287. doi: 10.1038/2011284a0. [DOI] [PubMed] [Google Scholar]
  9. HARTLEY B. S., KILBY B. A. The reaction of p-nitrophenyl esters with chymotrypsin and insulin. Biochem J. 1954 Feb;56(2):288–297. doi: 10.1042/bj0560288. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. HARTLEY B. S. Proteolytic enzymes. Annu Rev Biochem. 1960;29:45–72. doi: 10.1146/annurev.bi.29.070160.000401. [DOI] [PubMed] [Google Scholar]
  11. HEIN G., NIEMANN C. An interpretation of the kinetic behavior of model substrates of alpha-chymotrypsin. Proc Natl Acad Sci U S A. 1961 Sep 15;47:1341–1355. doi: 10.1073/pnas.47.9.1341. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. INAGAMI T., STURTEVANT J. M. Nonspecific catalyses by alpha-chymotrypsin and trypsin. J Biol Chem. 1960 Apr;235:1019–1023. [PubMed] [Google Scholar]
  13. JANSEN E. F., BALLS A. K. The inhibition of beta- and gamma-chymotrypsin and trypsin by diisopropyl fluorophosphate. J Biol Chem. 1952 Feb;194(2):721–727. [PubMed] [Google Scholar]
  14. KELLER P. J., COHEN E., NEURATH H. The proteins of bovine pancreatic juice. II. Rates of synthesis in vivo of the cationic proteins. J Biol Chem. 1959 Feb;234(2):311–315. [PubMed] [Google Scholar]
  15. KOSHLAND D. E., Jr, STRUMEYER D. H., RAY W. J., Jr Amino acids involved in the action of chymotrypsin. Brookhaven Symp Biol. 1962 Dec;15:101–133. [PubMed] [Google Scholar]
  16. MARGOLIASH E. PRIMARY STRUCTURE AND EVOLUTION OF CYTOCHROME C. Proc Natl Acad Sci U S A. 1963 Oct;50:672–679. doi: 10.1073/pnas.50.4.672. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. NEURATH H., DIXON G. H. Structure and activation of trypsinogen and chymotrypsinogen. Fed Proc. 1957 Sep;16(3):791–801. [PubMed] [Google Scholar]
  18. OOSTERBAAN R. A., VAN ADRICHEM M. E. Isolation of acetyl peptides from acetylchymotrypsin. Biochim Biophys Acta. 1958 Feb;27(2):423–425. doi: 10.1016/0006-3002(58)90359-7. [DOI] [PubMed] [Google Scholar]
  19. SCHAFFER N. K., MAY S. C., Jr, SUMMERSON W. H. Serine phosphoric acid from diisopropylphosphoryl chymotrypsin. J Biol Chem. 1953 May;202(1):67–76. [PubMed] [Google Scholar]
  20. SCHOELLMANN G., SHAW E. Direct evidence for the presence of histidine in the active center of chymotrypsin. Biochemistry. 1963 Mar-Apr;2:252–255. doi: 10.1021/bi00902a008. [DOI] [PubMed] [Google Scholar]
  21. SIEKEVITZ P., PALADE G. E. A cytochemical study on the pancreas of the guinea pig. 6. Release of enzymes and ribonucleic acid from ribonucleoprotein particles. J Biophys Biochem Cytol. 1960 Jul;7:631–644. doi: 10.1083/jcb.7.4.631. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. WALSH K. A., KAUFFMAN D. L., KUMAR K. S., NEURATH H. ON THE STRUCTURE AND FUNCTION OF BOVINE TRYPSINOGEN AND TRYPSIN. Proc Natl Acad Sci U S A. 1964 Feb;51:301–308. doi: 10.1073/pnas.51.2.301. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. WILLIAMS J., CLEGG J. B., MUTCH M. O. Coincidence and protein structure. J Mol Biol. 1961 Oct;3:532–540. doi: 10.1016/s0022-2836(61)80019-3. [DOI] [PubMed] [Google Scholar]

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