Abstract
Proteus mirabilis β -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 β -lactamase that extracted from isolate number 4TF and 20TF was 5.4.
Article Type
Article
How to Cite this Article
Al-Jumaily, Essam F.; Al-Taai, Hadi R.R.; Abbas, Ala'a S.; and Khanaeqah, Hussan H.
(2009)
"Isolation and purlfkation of β-lactemase from proteus mairbilis local isolates 4TF and 20TF,"
Baghdad Science Journal: Vol. 6:
Iss.
2, Article 2.
DOI: https://doi.org/10.21123/bsj.2009.6.2.249-256
