A comparative study of the conformational stabilities of trypsin and α-chymotrypsin

Acta Biologica Szegediensis

Volumn 45, Issue 1-4, 2001, Pages 43-49

  Simon, Mária L ^a   László, Kinga ^a   Kotormán, Márta ^a   Szajáni, Béla ^a  

^a UNIVERSITY OF SZEGED   (Hungary)

Author keywords

chymotrypsin; Autolysis; Conformational stability; pH effect; Trypsin

Indexed keywords

AMIDE; CHYMOTRYPSIN A; ESTER; TRYPSIN;

ARTICLE; AUTOLYSIS; CHEMICAL REACTION; COMPARATIVE STUDY; CONTROLLED STUDY; ENZYME ACTIVATION; ENZYME CONFORMATION; ENZYME DENATURATION; ENZYME INACTIVATION; ENZYME SUBSTRATE; HEAT; MOLECULAR STABILITY; PH; TEMPERATURE; TIME; VELOCITY;

EID: 0035698424     PISSN: 03246523     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article

References (22)

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2. Refined chrystal structure of γ-chymotrypsin in 1.9 A resolution
3. Étude thermodinamique de la denaturation termique réversible de la trypsine entre pH 1.0 et 3.4
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9. Converting trypsin to chymotrypsin: The role of surface loops
10. Catalytic properties of trypsin, Biological macromolecules and assemblies: Active site of enzymes
11. Trypsin
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13. Sur la morphologie des trypsines de porc et de bceuf étude des denaturations reversibles
14. Étude structurale du trypsinogéne et de la trypsine. Les diagrammes d'état
15. Photometric ninhydrin method for use in the chromatography of amino acids
16. Mechanism of protease action
17. A spectrophotometric determination of trypsin and chymotrypsin
18. Stability of hydrolytic enzymes in water-organic solvent systems
19. Structure of christalline α-chymotrypsin
20. Refolding transition of α-chymotrypsin: pH and salt dependence
21. Studies on self-association of proteins. The self-association of α-chymotrypsin at pH 8.3 and ionic strength 0.05
22. Serine proteases