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Isolation, Purification and Partial Characterisation of Urease from Seeds of Water Melon (Citrullus vulgaris)

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Abstract

Urease from seeds of water melon was purified to apparent homogeniety upto a sp act of 3750 units/mg protein with 31% recovery. Enzyme showed single protein band on native PAGE by urease specific staining. The mol wt of the enzyme was 4,70,000 and the preparation was free from bound nucleotides (A280/A260=1.14). The enzyme exhibited maximum activity in 50 mM Tris-acetate buffer (pH 8.5). The Km for urease was 8 mM. The enzyme was not inhibited by 25 mM of EDTA in 50 mM Tris-acetate buffer (pH 8.0 and 8.5).

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  1. Department of Biochemistry, Faculty of Science, Banaras Hindu University, Varanasi, 221 005, India

    Om Prakash & Gunjan Bhushan

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  1. Om Prakash
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  2. Gunjan Bhushan
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Prakash, O., Bhushan, G. Isolation, Purification and Partial Characterisation of Urease from Seeds of Water Melon (Citrullus vulgaris). J. Plant Biochem. Biotechnol. 6, 45–47 (1997). https://doi.org/10.1007/BF03263009

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  • DOI: https://doi.org/10.1007/BF03263009

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