Structure-Function Relationships of Proteolytic Enzymes (eBook, PDF)
Proceedings of the International Symposium, Copenhagen June 16-18, 1969, No. 37 in the Series of the International Union of Biochemistry Sponsored Symposia
Redaktion: Desnuelle, P.; Ottesen, M.; Neurath, H.
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Structure-Function Relationships of Proteolytic Enzymes provides information pertinent to the fundamental aspects of proteolytic enzymes. This book presents the historical role of proteolytic enzyme as a group in protein and enzyme chemistry.Organized into 23 chapters, this book begins with an overview of the results obtained from investigation on the chymotrypsinogens of porcine origin. This text then examines the differences of amino acid sequence between chymotrypsin, trypsin, and elastase that affect the substrate binding site, which reflect the specificity differences between these enzyme...
Structure-Function Relationships of Proteolytic Enzymes provides information pertinent to the fundamental aspects of proteolytic enzymes. This book presents the historical role of proteolytic enzyme as a group in protein and enzyme chemistry.
Organized into 23 chapters, this book begins with an overview of the results obtained from investigation on the chymotrypsinogens of porcine origin. This text then examines the differences of amino acid sequence between chymotrypsin, trypsin, and elastase that affect the substrate binding site, which reflect the specificity differences between these enzymes. Other chapters consider the kinetic parameters related to the trypsin-catalyzed hydrolysis of several model peptides. This book discusses as well the acetylation of trypsin, which result in functional consequences varying from complete inactivation to promotion of activity. The final chapter deals with the physical properties of stem bromelain in comparison with the data for three other sulfhydryl proteases of plant origin.
This book is a valuable resource for enzymologists, microbiologists, and biochemists.
Organized into 23 chapters, this book begins with an overview of the results obtained from investigation on the chymotrypsinogens of porcine origin. This text then examines the differences of amino acid sequence between chymotrypsin, trypsin, and elastase that affect the substrate binding site, which reflect the specificity differences between these enzymes. Other chapters consider the kinetic parameters related to the trypsin-catalyzed hydrolysis of several model peptides. This book discusses as well the acetylation of trypsin, which result in functional consequences varying from complete inactivation to promotion of activity. The final chapter deals with the physical properties of stem bromelain in comparison with the data for three other sulfhydryl proteases of plant origin.
This book is a valuable resource for enzymologists, microbiologists, and biochemists.
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