상세 정보

underline
Metadata Downloads : dc(xml) or Excel
Cited 0 time in scopus ci

Title 

Identification of a serine protease from a Bacillus sp. using multiple loading of O'Farrell-type isolectric focusing slab two-dimensinal gel

 

바실러스 유래의 세린 프로티아제의 규명

Authors 

Nack-Shick ChoiJong Hyun ChoiJung-Hoon YoonSeung Goo LeeJae Jun Song

Publisher 

Springer Verlag (Germany)

Issue Date 

2009

Citation 

Biotechnology Letters, vol. 31, no. 7, pp. 975-978

Keywords 

isoelectric focusingMALDI-TOF/MSproteasetwo-dimensional electrophoresiszymography

Abstract 

A protease was purified from Bacillus sp. DJ isolated from Doenjang, a traditional Korean fermented food. Its molecular weight (MW) and isoelectric point (p I) were 18-19 kDa and 6.0-6.5 using 1- or 2-D fibrin zymography, respectively. The protease was optimally active at pH 9 and 55°C. Activity was inhibited by 1 mM PMSF, but not by EDTA, EGTA, aprotinin, or leupeptin, indicating that the protease is a serine protease. By using a new electrophoretic technique, multiple loading of O'Farrell-type isoelectric focusing (IEF) slab gel, the first amino acid residues of the N-terminal sequence of the protease were determined as HPLVLVDPIL, which is 80% identical with serine proteases of the subtilase family.

ISSN 

0141-5492

Link 

http://dx.doi.org/10.1007/s10529-009-9962-z

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2019-05-02


There are no files associated with this item.
qrcode

FusionCharts.
DSpace Software Coptright(c) 2010 MIT and Hewleft-Packard  /  KRIBB-REPOSITORY ( Email:jakim@kribb.re.kr)