Identification of a serine protease from a Bacillus sp. using multiple loading of O'Farrell-type isoelectric focusing slab two-dimensional gel.Biotechnol Lett. 2009 Jul; 31(7):975-8.BL
Abstract
A protease was purified from Bacillus sp. DJ isolated from Doenjang, a traditional Korean fermented food. Its molecular weight (MW) and isoelectric point (pI) 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 degrees 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.
Links
MeSH
Pub Type(s)
Journal Article
Research Support, Non-U.S. Gov't
Language
eng
PubMed ID
19271156
Citation
Choi, Nack-Shick, et al. "Identification of a Serine Protease From a Bacillus Sp. Using Multiple Loading of O'Farrell-type Isoelectric Focusing Slab Two-dimensional Gel." Biotechnology Letters, vol. 31, no. 7, 2009, pp. 975-8.
Choi NS, Choi JH, Yoon JH, et al. Identification of a serine protease from a Bacillus sp. using multiple loading of O'Farrell-type isoelectric focusing slab two-dimensional gel. Biotechnol Lett. 2009;31(7):975-8.
Choi, N. S., Choi, J. H., Yoon, J. H., Lee, S. G., & Song, J. J. (2009). Identification of a serine protease from a Bacillus sp. using multiple loading of O'Farrell-type isoelectric focusing slab two-dimensional gel. Biotechnology Letters, 31(7), 975-8. https://doi.org/10.1007/s10529-009-9962-z
Choi NS, et al. Identification of a Serine Protease From a Bacillus Sp. Using Multiple Loading of O'Farrell-type Isoelectric Focusing Slab Two-dimensional Gel. Biotechnol Lett. 2009;31(7):975-8. PubMed PMID: 19271156.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR
T1 - Identification of a serine protease from a Bacillus sp. using multiple loading of O'Farrell-type isoelectric focusing slab two-dimensional gel.
AU - Choi,Nack-Shick,
AU - Choi,Jong Hyun,
AU - Yoon,Jung-Hoon,
AU - Lee,Seung-Goo,
AU - Song,Jae Jun,
Y1 - 2009/03/07/
PY - 2008/10/28/received
PY - 2009/02/03/accepted
PY - 2009/02/02/revised
PY - 2009/3/10/entrez
PY - 2009/3/10/pubmed
PY - 2009/7/29/medline
SP - 975
EP - 8
JF - Biotechnology letters
JO - Biotechnol Lett
VL - 31
IS - 7
N2 - A protease was purified from Bacillus sp. DJ isolated from Doenjang, a traditional Korean fermented food. Its molecular weight (MW) and isoelectric point (pI) 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 degrees 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.
SN - 1573-6776
UR - https://www.unboundmedicine.com/medline/citation/19271156/Identification_of_a_serine_protease_from_a_Bacillus_sp__using_multiple_loading_of_O'Farrell_type_isoelectric_focusing_slab_two_dimensional_gel_
L2 - https://doi.org/10.1007/s10529-009-9962-z
DB - PRIME
DP - Unbound Medicine
ER -