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Journal Abstract Search
114 related items for PubMed ID: 4811900
1. Specificities of alpha-chymotrypsin and subtilisin Carlsberg. The alpha-acylamido effect in beta-phenylpropionates and their rigid analogs. Matta MS, Staley DD. J Biol Chem; 1974 Feb 10; 249(3):732-7. PubMed ID: 4811900 [No Abstract] [Full Text] [Related]
2. The topographical differences in the active site region of alpha-chymotrypsin, subtilisin Novo, and subtilisin Carlsberg. Mapping the aromatic binding site by inhibitors (virtual substrates). Bosshard HR, Berger A. Biochemistry; 1974 Jan 15; 13(2):266-77. PubMed ID: 4810052 [No Abstract] [Full Text] [Related]
3. Specificity of -chymotrypsin. Separation of polar, steric, and specific effects in the -chymotrypsin-catalyzed hydrolysis of acyl-substituted p-nitrophenyl esters. Dupaix A, Béchet JJ, Roucous C. Biochemistry; 1973 Jul 03; 12(14):2559-66. PubMed ID: 4711463 [No Abstract] [Full Text] [Related]
4. Kinetic specificities of BPN' and Carlsberg subtilisins. Mapping the aromatic binding site. Karasaki Y, Ohno M. J Biochem; 1978 Sep 03; 84(3):531-8. PubMed ID: 102640 [Abstract] [Full Text] [Related]
5. Alpha-chymotrypsin and rigid substrates. Reactivity of some p-nitrophenyl 1,2,3,4-tetrahydro-2-naphthoates and indan-2-carboxylates. Matta MS, Rohde MF. J Am Chem Soc; 1972 Nov 29; 94(24):8573-8. PubMed ID: 4638989 [No Abstract] [Full Text] [Related]
6. Subtilisin-catalyzed hydrolysis of peptide methyl esters. Philipp M, Bender ML. FEBS Lett; 1974 Jun 15; 42(3):282-4. PubMed ID: 4854515 [No Abstract] [Full Text] [Related]
7. Symmetry and asymmetry in the mechanisms of hydrolysis by serine proteases and their thiol analogues. Polgár L. Acta Biochim Biophys Acad Sci Hung; 1972 Jun 15; 7(4):319-34. PubMed ID: 4671999 [No Abstract] [Full Text] [Related]
8. Kinetic investigation of the alpha-chymotrypsin-catalyzed hydrolysis of peptide substrates. The relationship between peptide-structure N-terminal to the cleaved bond and reactivity. Baumann WK, Bizzozero SA, Dutler H. Eur J Biochem; 1973 Nov 15; 39(2):381-91. PubMed ID: 4775056 [No Abstract] [Full Text] [Related]
9. Interactions of alpha-chymotrypsin and Carlsberg subtilisin with methyl N alpha-acetyl-2-(alkylthio)-L-tryptophanoates. Yoshizumi K, Kamiyama K, Shieh TC, Tanaka S, Ohno M. J Biochem; 1986 Nov 15; 100(5):1201-6. PubMed ID: 3546277 [Abstract] [Full Text] [Related]
10. Binding of the recombinant proteinase inhibitor eglin c from leech Hirudo medicinalis to human leukocyte elastase, bovine alpha-chymotrypsin and subtilisin Carlsberg: thermodynamic study. Ascenzi P, Amiconi G, Menegatti E, Guarneri M, Bolognesi M, Schnebli HP. J Enzyme Inhib; 1988 Nov 15; 2(3):167-72. PubMed ID: 3071573 [Abstract] [Full Text] [Related]
11. Specificity of -chymotrypsin. The -chymotrypsin-catalyzed hydrolysis of N-acylamino acid p-nitrophenyl esters. Béchet JJ, Dupaix A, Roucous C. Biochemistry; 1973 Jul 03; 12(14):2566-72. PubMed ID: 4711464 [No Abstract] [Full Text] [Related]
12. Structural comparison of two serine proteinase-protein inhibitor complexes: eglin-c-subtilisin Carlsberg and CI-2-subtilisin Novo. McPhalen CA, James MN. Biochemistry; 1988 Aug 23; 27(17):6582-98. PubMed ID: 3064813 [Abstract] [Full Text] [Related]
13. The binding of specific and non-specific aldehyde substrate analogs to alpha-chymotrypsin. Breaux EJ, Bender ML. FEBS Lett; 1975 Aug 01; 56(1):81-4. PubMed ID: 239865 [No Abstract] [Full Text] [Related]
14. Change in the conformation of delta-chymotrypin upon binding a specific substrate at high pH. Garel JR. FEBS Lett; 1975 Feb 15; 50(3):339-45. PubMed ID: 234861 [No Abstract] [Full Text] [Related]
16. Stereochemistry of the active site of -chymotrypsin. The influence of polar groups in locked substrates. Pattabiraman TN, Lawson WB. J Biol Chem; 1972 May 25; 247(10):3029-38. PubMed ID: 5027740 [No Abstract] [Full Text] [Related]
19. Use of N-benzoyl-L-tyrosine thiobenzyl ester as a protease substrate. Hydrolysis by alpha-chymotrypsin and subtilisin BPN. Farmer DA, Hageman JH. J Biol Chem; 1975 Sep 25; 250(18):7366-71. PubMed ID: 240825 [Abstract] [Full Text] [Related]