Abstract:
:The clottable protein (CP) was isolated from white shrimp, Penaeus vannamei plasma as a 400-kDa protein that splits to two identical 200-kDa subunits when it is reduced with 2-ME. However, using DTT as reducing agent, four main bands were observed; two of them (179 and 125 kDa) had the same N-terminus sequence of the intact CP, indicating that most fragmentation occurs in the carboxy-terminus. The proteinase activity of reduced CP was detected using azoalbumin as substrate. Proteinase activity was only detected in the reduced, but not alkylated protein. Trypsin and papain, as well as soybean trypsin inhibitor and E64, were included for comparison. Proteolytic activity of reduced CP was inhibited by E64, but not by STI, indicating that such activity corresponds to a cysteine type proteinase.
journal_name
Biochem Biophys Res Communjournal_title
Biochemical and biophysical research communicationsauthors
Reyes-Izquierdo T,Vargas-Albores Fdoi
10.1006/bbrc.2001.5595subject
Has Abstractpub_date
2001-09-21 00:00:00pages
332-6issue
2eissn
0006-291Xissn
1090-2104pii
S0006-291X(01)95595-0journal_volume
287pub_type
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