clostripain


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clos·tri·pain

(klos'tri-pān),
A cysteine proteinase cleaving preferentially at the carboxyl side of arginyl and lysyl residues. It also has an esterase activity.
References in periodicals archive ?
There are different types of proteases which differ on their source type, some of which includes ficain, asclepian, papain, clostripain etc.
Table 2 Summary of proteolytic cleavage sites in SNARE proteins and synaptotagmin Total Number of Protease Cleavage Sites Trypsin Papain Clostripain Protein Number Ave Min Ave Min Ave Min of Isoforms Analyzed Syntaxin 94 42 29 81 53 20 6 SNAP25 25 12 8 25 20 6 5 (N[H.sub.2]-term) SNAP25 (C-term) 25 17 10 37 17 8 5 Synaptobrevin 73 19 12 42 23 9 4 Synaptotagmin 59 63 42 134 77 22 4 Number of Amino Acids From Transmernbrane Region to First Cleavage Site Protein Trypsin Papain Clostripain Ave Min Ave Max Ave Max Syntaxin 3 4 3 4 6 14 SNAP25 4 6 3 6 21 29 (N[H.sub.2]-term) SNAP25 (C-term) 3 6 3 6 9 14 Synaptobrevin 9 11 9 11 11 63 Synaptotagmin 5 9 4 6 35 161 Amino acids are counted from the N[H.sub.2] and C--terminal sides of the palmiloylated cysteine residues in the center of SNAP25.
However, after limited proteolysis of PSA by trypsin, [alpha]-chymotrypsin, clostripain, or V8 protease, the resulting PSA proteolytic fragments were not immunoreactive as evidenced by Western blot analysis under reducing as well as nonreducing conditions (data not shown).