Acid Proteases - Tang Jordan
Acid Proteases - Tang Jordan
- Structure, Function, and Biology
EAN: 9781475707205
Marka
Symbol
574HJI03527KS
Rok wydania
2013
Strony
370
Oprawa
Miekka
Format
17.0x24.4cm
Redakcja
Tang Jordan
Język
angielski

Bez ryzyka
14 dni na łatwy zwrot

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Marka
Symbol
574HJI03527KS
Kod producenta
9781475707205
Rok wydania
2013
Strony
370
Oprawa
Miekka
Format
17.0x24.4cm
Redakcja
Tang Jordan
Język
angielski

In the past ten years, a number of proceedings of symposia on the structure and function of proteolytic enzymes have been pub lished. Their coverage of acid proteases has been limited, mainly due to the lack of significant new information on the structure of these enzymes. In the last four years, however, the primary and tertiary structures of a number of acid proteases have been deter mined, prompting the need to discuss the meanings of the old data and the possibilities for new experimentations. It was for this purpose that the "Conference on Acid Proteases: Structure, Function, and Biology" was organized. It took place at the University of Oklahoma on November 21-24, 1976. This book is a collection of the main lectures delivered at the Conference. Acid Proteases, by definition refers to a group of proteases having an optimal pH in acidic solutions. The classic examples are pepsin and chymosin. Some catalytic features are obviously shared by these proteases, most notably, their inhibition by pepstatin. The use of active center-directed inactivators such as diazoacetyl norleucine methyl ester and 1,2-epoxy-3-(p-nitrophenoxy)propane has shown that two catalytic aspartyl residues are present in most of these enzymes. These apparent cornmon features have prompted the suggestion by several investigators to name this group of enzymes "aspartyl proteases" or "carboxyl proteases".
EAN: 9781475707205
EAN: 9781475707205
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