Thermal Stability of Immobilized Enzymes Circular Dichroism, Fluorescence and Kinetic Measurements of α‐Chymotrypsin Attached to Soluble Carriers

The temperature‐induced unfolding of α‐chymotrypsin and of chymotrypsin covalently bound to two soluble transparent carriers, dextran and a copolymer of maleic acid anhydride and acrylic acid, has been studied by tryptophan fluorescence emission, circular dichroic and kinetic measurements. It has be...

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Veröffentlicht in:	European journal of biochemistry 1976-04, Vol.63 (2), p.591-598
Hauptverfasser:	LASCH, Jürgen, BESSMERTNAYA, Ludmila, KOZLOV, Leonid V., ANTONOV, Vladimir K.
Format:	Artikel
Sprache:	eng
Schlagworte:	Acrylates Binding Sites Chymotrypsin - metabolism Circular Dichroism Computers Dextrans Drug Stability Hot Temperature Kinetics Maleates Protein Binding Protein Conformation Spectrometry, Fluorescence
Online-Zugang:	Volltext
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