Open AccessIsolation and purlfkation of B-lactemase from proteus mairbilis local isolates 4TF and 20TF
Author(s) -
Baghdad Science Journal
Publication year - 2009
Publication title -
mağallaẗ baġdād li-l-ʿulūm
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.167
H-Index - 6
eISSN - 2411-7986
pISSN - 2078-8665
DOI - 10.21123/bsj.6.2.249-256
Subject(s) - isoelectric point , proteus mirabilis , proteus , isolation (microbiology) , isoelectric focusing , microbiology and biotechnology , size exclusion chromatography , chemistry , biology , enzyme , chromatography , biochemistry , escherichia coli , gene
Proteus mirabilis ? -lactamase of local isolates number 4TF represent karkh side and 20TF represent rusafa side of Baghdad were extracted and purified 23.17, 25.23 fold with yield of 36.66 %, 37.5% and specific activity 11.8, 12.6 of unit/ mg protein by DEAE –cellulose and Sepharose 4B (respectively ).Molecular weight of both enzyme was about 35500 Dalton determined by gel filtration. The study indicated that the isoelectric point of purified ? -lactamase that extracted from isolate number 4TF and 20TF was 5.4.