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clostripain

Known as: clostridiopeptiase B 
 
National Institutes of Health

Papers overview

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Highly Cited
2000
Highly Cited
2000
This study describes the relationship between the solubility of glycinin, a major soy protein, and its structural properties at a… Expand
Highly Cited
1999
Highly Cited
1999
Photoaffinity labeling methods have allowed a definition of the sites of interaction between Taxol and its cellular target, the… Expand
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Highly Cited
1998
Highly Cited
1998
We show by site‐directed mutagenesis that the catalytic residues of mammalian legumain, a recently discovered lysosomal… Expand
Highly Cited
1994
Highly Cited
1994
An improved and simplified procedure for enzymatic digestion of proteins bound to polyvinylidene difluoride (PVDF) membranes for… Expand
1991
1991
In view of the probability that clostripain (EC 3,4,22.8) is fundamentally different in structure from other known cysteine… Expand
Highly Cited
1989
Highly Cited
1989
Limited proteolysis of calcineurin, the Ca2+/calmodulin-stimulated protein phosphatase, with clostripain is sequential and… Expand
1986
1986
Rat liver chromatin core particles digested with clostripain yield a structurally well‐defined nucleoprotein particle with an… Expand
Highly Cited
1979
Highly Cited
1979
A highly active form of clostripain, composed of two polypeptide chains (Mr = 43,000 and 12,500), was isolated by hydrophobic… Expand
1971
1971
Abstract Clostripain is rapidly and selectively inactivated by the chloromethyl ketone derived from α-N-tosyl-l-lysine (TLCK… Expand
Highly Cited
1968
Highly Cited
1968
Abstract The proteolytic enzyme, clostridiopeptidase B (clostripain), from Clostridium histolyticum culture filtrates has been… Expand
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