Isolation and purlfkation of B-lactemase from proteus mairbilis local isolates 4TF and 20TF
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 (respectivel...
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| Main Author: | |
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| Format: | Article |
| Language: | English |
| Published: |
University of Baghdad, College of Science for Women
2009-06-01
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| Series: | مجلة بغداد للعلوم |
| Subjects: | |
| Online Access: | http://bsj.uobaghdad.edu.iq/index.php/BSJ/article/view/977 |
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| Summary: | 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. |
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| ISSN: | 2078-8665 2411-7986 |