EC Number   |
Application |
Reference |
|---|
  3.4.22.8 | medicine |
influence of protease inhibitors aprotinin, phenylmethylsulfonyl fluoride, L-1-chloro-3-[4-tosylamido]-7-amino-2-heptanone, and chymostatin on toxicity of Clostridium histolyticum supernatant towards HeLa cells. Aprotinin has no effect, while the other inhibitors potentiate the cytotoxic activity of Clostridium histolyticum probybly by hindering the natural defense of cells. In addition, phenylmethylsulfonyl fluoride and L-1-chloro-3-[4-tosylamido]-7-amino-2-heptanone block clostripain enzymic activity |
668643 |
| 3.4.22.8 | medicine |
it is possible to isolate significant numbers of human islets combining collagenase only with clostripain. The supplementation with clostripain is an effective means to substantially reduce neutral protease activity, which significantly decreases survival and viability after culture |
753211 |
| 3.4.22.8 | medicine |
neutral protease derived from Clostridium histolyticum and clostripain, in combination with collagenase derived from the same bacteria, may effectively increase the isolation efficiency of pancreatic islet without affecting the quality of islets |
755618 |
| 3.4.22.8 | medicine |
the addition of clostripain to the enzyme blend soundly improves islet yields and transplantation rates. It gently aids pancreas digestion and maintained proper islet functionality. The addition of clostripain to the enzyme blend is implemented into standard isolation protocols at the isolation centers in Uppsala and in Oslo |
755617 |
| 3.4.22.8 | synthesis |
efficient biocatalyst for the synthesis of peptide isosteres |
652992 |
| 3.4.22.8 | synthesis |
recombinant clostripain might prove useful in the production of insulin from the proinsulin fusion protein |
687876 |
| 3.4.22.8 | synthesis |
the enzyme can be used for the high yielding synthesis of a variety of peptide bond using L-Arg and, to a lesser degree, L-Lys as substrates with L-amino acid amides or D-amino acid amides |
81580 |
