Sanaa T. El-Sayed
Biochemistry Department, National Research Center, Tahrir St, Dokki, Cairo, Egypt
Ahmed M. Salem
Biochemistry Department, Faculty of Science, Ain Shams University, Egypt
Abeer N. Shehata
Biochemistry Department, National Research Center, Tahrir St, Dokki, Cairo, Egypt
Etidal W. Jwanny
Biochemistry Department, National Research Center, Tahrir St, Dokki, Cairo, Egypt
Chitinase from leaves of sugar beet was purified by (NH4)2SO4 precipitation (20-60%) and fractionated on Sephadex G-120 followed by Sephadex G-200 column chromatography. A 18.9 fold purification of the enzyme with 14.0 ImU/mg specific activity was achieved. The yield of the purified chitinase was 43.4 mg protein (608 ImU) from 100g dry leaves tissues. The prepared enzyme was showing a single protein band on agarose gel electrophoresis. The purified enzyme had been shown to have a M, 64×103 Dalton on the basis of gel filtration on Sephadex G-200 column. Optimum chitinase activity on chitin was recorded in 0.1M acetate buffer, pH 4.5 at 40°C.
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How to cite this article
Sanaa T. El-Sayed, Ahmed M. Salem, Abeer N. Shehata and Etidal W. Jwanny, 2000. Chitinase from Leaves of Beta vulgaris and other Higher Plants. Pakistan Journal of Biological Sciences, 3: 250-256.
DOI: 10.3923/pjbs.2000.250.256
URL: https://scialert.net/abstract/?doi=pjbs.2000.250.256
DOI: 10.3923/pjbs.2000.250.256
URL: https://scialert.net/abstract/?doi=pjbs.2000.250.256