Comparative study of enzyme activity and stability of bovine and human plasmins in electrophoretic reagents, β-mercaptoethanol, DTT, SDS, Triton X-100, and Urea

Cited 0 time in scopus
Metadata Downloads
Title
Comparative study of enzyme activity and stability of bovine and human plasmins in electrophoretic reagents, β-mercaptoethanol, DTT, SDS, Triton X-100, and Urea
Author(s)
Nack Shick Choi; Jeung Ho Hahm; P J Maeng; Seung Ho Kim
Bibliographic Citation
BMB Reports, vol. 38, no. 2, pp. 177-181
Publication Year
2005
Abstract
Effects of common electrophoretic reagents, reducing agents (β-mercaptoethanol [BME] and DTT), denaturants (SDS and urea), and non-ionic detergent (Triton X-100), on the activity and stability of bovine plasmin (b-pln) and human plasmin (h-pln) were compared. In the presence of 0.1% SDS (w/v), all reagents completely inhibited two plns, whereas SDS (1%) and urea (1 M) denatured plns recovered their activities after removal of SDS by treatment of 2.5% Triton X-100 (v/v). However, reducing agents (0.1 M of BME and DTT) treated plns did not restore their activities. Based on a fibrin zymogram gel, five (from b-pln) and four (from h-pln) active fragments were resolved. Two plns exhibited unusual stability in concentrated SDS and Triton X-100 (final 10%) and urea (final 6 M) solutions. Two bands, heavy chain-2 (HC-2) and cleaved heavy chain-2 (CHC-2), of b-pln were completely inhibited in 0.5% SDS or 3 M urea, whereas no significant difference was found in h-pln. Interestingly, 50 kDa (cleaved heavy chain-1, CHC-1) of b-pln and two fragments, 26 kDa (light chain, LC) and 29 kDa (microplasmin, MP), of h-pln were increased by SDS in a concentration dependent manner. We also found that the inhibition of SDS against both plns was reversible.
Keyword
denaturantfibrin platefibrinolysisplasminzymography
ISSN
1225-8687
Publisher
Korea Soc-Assoc-Inst
Type
Article
Appears in Collections:
1. Journal Articles > Journal Articles
Files in This Item:
  • There are no files associated with this item.


Items in OpenAccess@KRIBB are protected by copyright, with all rights reserved, unless otherwise indicated.