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Purification and Biochemical Characterisation of Acid phosphatase-I From Seeds of Nelumbo Nucifera

Purification and Biochemical Characterisation of Acid phosphatase-I From Seeds of Nelumbo Nucifera

Sanaullah Khan, Shahnaz Khan, Sajida Batool, Mushtaq Ahmed

Nat Prod Res. 2016;30(5):570-3.

PMID: 25887488

Abstract:

Acid phosphatase-I (Apase-I) from seeds of Nelumbo nucifera was purified to electrophoretic homogeneity by combination of ammonium sulfate precipitation, size-exclusion and ion exchange chromatography. SDS-PAGE of purified Apase-I gave a single band with molecular mass of 80 kDa under reducing and non-reducing conditions, indicating that the enzyme was a monomer. The purified enzyme showed maximum activity at 50°C and at pH 5. The Km, Vmax and Kcat for p-nitrophenyl phosphate were 132 μM, 10 μmol/min/mg and 6.7/sec respectively. Apase-I activity was strongly inhibited by Zn(2+), W(2+); weakly inhibited by Cu(2+), Mo(2+) and Cr(6+) and moderately activated by Mg(2+). The enzyme was shown to be thermolabile as it lost 50% of its activity at 50°C after incubation for 1 hour. The amino acid analysis of enzyme revealed high proportion of acidic amino acids, which is very similar to that of tomato Apase-I and lower than potato Apase.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
AP9001778-A	Phosphatase, Acid from potato		9001-77-8	Price

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