Isolation and purlfkation of B-lactemase from proteus mairbilis local isolates 4TF and 20TF

محتوى المقالة الرئيسي

Essam F. Al-Jumaily
Hadi R.R. Al-Taai
Ala'a S. Abbas
Hussan H. Khanaeqah

الملخص

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.

تفاصيل المقالة

كيفية الاقتباس
1.
Isolation and purlfkation of B-lactemase from proteus mairbilis local isolates 4TF and 20TF. Baghdad Sci.J [انترنت]. 7 يونيو، 2009 [وثق 17 مايو، 2024];6(2):249-56. موجود في: https://bsj.uobaghdad.edu.iq/index.php/BSJ/article/view/977
القسم
article

كيفية الاقتباس

1.
Isolation and purlfkation of B-lactemase from proteus mairbilis local isolates 4TF and 20TF. Baghdad Sci.J [انترنت]. 7 يونيو، 2009 [وثق 17 مايو، 2024];6(2):249-56. موجود في: https://bsj.uobaghdad.edu.iq/index.php/BSJ/article/view/977

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