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rhizopuspepsin

Known as: Rhizopus carboxyl proteinase, rhizopepsin, Rhizopus chinensis aspartic protease 
 
National Institutes of Health

Papers overview

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2009
2009
Hydrogen/deuterium (H/D) exchange coupled to mass spectrometry is nowadays routinely used to probe protein interactions or… Expand
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2009
2009
A secretory aspartic protease (also termed as rhizopuspepsin) was purified from Rhizopus oryzae NBRC 4749 by ion exchange… Expand
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1995
1995
Rhizopuspepsin and other fungal aspartic proteinases are distinct from the mammalian enzymes in that they are able to cleave… Expand
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Highly Cited
1993
Highly Cited
1993
Cathepsin D (EC 3.4.23.5) is a lysosomal protease suspected to play important roles in protein catabolism, antigen processing… Expand
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1992
1992
The pH dependence of the kinetic parameters of pepsin, rhizopuspepsin, and their active-site hydrogen bond mutants has been… Expand
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1990
1990
The molecular structure of endothiapepsin (EC 3.4.23.6), the aspartic proteinase from Endothia parasitica, has been refined to a… Expand
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1989
1989
A detailed and rule-based side-chain modelling procedure for globular proteins is presented. It uses the conformational… Expand
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1988
1988
A gene encoding Rhizopus niveus aspartic proteinase was isolated from an R. niveus genomic library by using oligonucleotides… Expand
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1987
1987
The complete amino acid sequence of an aspartic protease from Rhizopus chinensis, rhizopuspepsin isozyme pI 5, has been… Expand
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1982
1982
1. Rhizopuspepsin has been purified from liquid cultures of Rhizopus chinensis. 2. Purification by ammonium sulfate precipitation… Expand
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