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. 1967 Jul;58(1):304–311. doi: 10.1073/pnas.58.1.304

Pi-, delta-, and gamma-chymotrypsin: three-dimensional electron-density and difference maps at 5 A resolution, and comparison with chymotrypsinogen.

J Kraut, H T Wright, M Kellerman, S T Freer
PMCID: PMC335634  PMID: 5231611

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Selected References

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

  1. Bernhard S. A., Lee B. F., Tashjian Z. H. On the interaction of the active side of alpha-chymotrypsin with chromophores: proflavin binding and enzyme conformation during catalysis. J Mol Biol. 1966 Jul;18(3):405–420. doi: 10.1016/s0022-2836(66)80033-5. [DOI] [PubMed] [Google Scholar]
  2. Biltonen R., Lumry R., Madison V., Parker H. Studies of the chymotrypsinogen family. IV. The conversion of chymotrypsinogen A to alpha-chymotrypsin. Proc Natl Acad Sci U S A. 1965 Nov;54(5):1412–1419. doi: 10.1073/pnas.54.5.1412. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. COREY R. B., BATTFAY O., BRUECKNER D. A., MAR F. G. PRELIMINARY X-RAY DIFFRACTION STUDIES OF CRYSTAL FORMS OF FREE AND INHIBITED CHYMOTRYPSIN. Biochim Biophys Acta. 1965 Mar 29;94:535–545. doi: 10.1016/0926-6585(65)90062-2. [DOI] [PubMed] [Google Scholar]
  4. DREYER W. J., NEURATH H., RUPLEY J. A. Structural changes in the activation of chymotrypsinogen and trypsinogen; effect of urea on chymotrypsinogen and delta-chymotrypsin. Arch Biochem Biophys. 1956 Nov;65(1):243–259. doi: 10.1016/0003-9861(56)90191-6. [DOI] [PubMed] [Google Scholar]
  5. Fasman G. D., Foster R. J., Beychok S. The conformational transition associated with the activation of chymotrypsinogen to chymotrypsin. J Mol Biol. 1966 Aug;19(2):240–253. doi: 10.1016/s0022-2836(66)80002-5. [DOI] [PubMed] [Google Scholar]
  6. GOLD A. M. SULFONYL FLUORIDES AS INHIBITORS OF ESTERASES. 3. IDENTIFICATION OF SERINE AS THE SITE OF SULFONYLATION IN PHENYLMETHANESULFONYL ALPHA-CHYMOTRYPSIN. Biochemistry. 1965 May;4:897–901. doi: 10.1021/bi00881a016. [DOI] [PubMed] [Google Scholar]
  7. Hartley B. S., Kauffman D. L. Corrections to the amino acid sequence of bovine chymotrypsinogen A. Biochem J. 1966 Oct;101(1):229–231. doi: 10.1042/bj1010229. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Himoe A., Parks P. C., Hess G. P. Investigations of the chymotrypsin-catalyzed hydrolysis of specific substrates. I. The pH dependence of the catalytic hydrolysis of N-acetyl-L-tryptophanamide by three forms of the enzyme at alkaline pH. J Biol Chem. 1967 Mar 10;242(5):919–929. [PubMed] [Google Scholar]
  9. KRAUT J., HIGH D. F., SIEKER L. C. CHYMOTRYPSINOGEN: INCREASED RESOLUTION AND ABSOLUTE CONFIGURATION. Proc Natl Acad Sci U S A. 1964 May;51:839–845. doi: 10.1073/pnas.51.5.839. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. KRAUT J., SIEKER L. C., HIGH D. F., FREER S. T. Chymotrypsinogen: a three-dimensional fourier synthesis at 5 angstrom resolution. Proc Natl Acad Sci U S A. 1962 Aug;48:1417–1424. doi: 10.1073/pnas.48.8.1417. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Meloun B., Kluh I., Kostka V., Morávek L., Prusík Z., Vanecek J., Keil B., Sorm F. Covalent structure of bovine chymotrypsinogen A. Biochim Biophys Acta. 1966 Dec 28;130(2):543–546. doi: 10.1016/0304-4165(66)90258-3. [DOI] [PubMed] [Google Scholar]
  12. Oppenheimer H. L., Labouesse B., Hess G. P. Implication of an ionizing group in the control of conformation and activity of chymotrypsin. J Biol Chem. 1966 Jun 10;241(11):2720–2730. [PubMed] [Google Scholar]
  13. ROVERY M., POILROUX M., YOSHIDA A., DESNUELLE P. Sur la dégradation du chymotrypsinogène par la chymotrypsine. Biochim Biophys Acta. 1957 Mar;23(3):608–620. doi: 10.1016/0006-3002(57)90383-9. [DOI] [PubMed] [Google Scholar]
  14. Raval D. N., Schellman J. A. The activation of chymotrypsinogen. Optical rotation studies. Biochim Biophys Acta. 1965 Oct 18;107(3):463–470. doi: 10.1016/0304-4165(65)90190-x. [DOI] [PubMed] [Google Scholar]
  15. SIGLER P. B., SKINNER H. C., COULTER C. L., KALLOS J., BRAXTON H., DAVIES D. R. AN ISOMORPHOUS HEAVY ATOM SUBSTITUTION AT THE ACTIVE SITE OF GAMMA-CHYMOTRYPSIN. Proc Natl Acad Sci U S A. 1964 Jun;51:1146–1151. doi: 10.1073/pnas.51.6.1146. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Weiner H., Koshland D. E., Jr Conformational studies on the interaction of chymotrypsin with substrates and inhibitors. J Mol Biol. 1965 Jul;12(3):881–891. doi: 10.1016/s0022-2836(65)80335-7. [DOI] [PubMed] [Google Scholar]

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