Isolation and purlfkation of B-lactemase from proteus mairbilis local isolates 4TF and 20TF
Keyword(s):
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.
2011 ◽
Vol 14
(3)
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pp. 5-11
Purification and some properties of pectinesterase from potato (Solanum tuberosum L.) alpha cultivar
2000 ◽
Vol 43
(4)
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pp. 393-398
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1984 ◽
Vol 62
(5)
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pp. 276-279
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