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2012•Journal of the chemical society of pakistanRequires access

Isolation, Purification and Characterization of Acid Phosphatase from Germinating Vigna radiata Seeds

Sadia Nadir, Asma Saeed, Rubina Naz, Aisha Siddiqua, Mehrin Sherazi, Sultan Mehmood Wazir, Ahmad Saeed, Ismail Alam Khan

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Abstract

of protein was obtained with recovery of nearly 1%. About 222 times purification was achieved. Sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE) resolved two bands of acid phosphatase corresponding to molecular weight of 29 kilo Dalton (kDa) and 18 kDa. The molecular weights of native enzyme determined by gel filtration on calibrated Sephadex G-100 column were found to be 29 kDa and 18 kDa The apparent Km value of 29 kDa isoenzyme with p-nitrophenyl phosphate (pNPP) as substrate was 0.3 mM and Vmax was 1336 nmol.sec -1 .mg -1 of protein. The optimal pH for this enzyme was 5.5 and pH stability was 4-7. It had optimum temperature of 50 o

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of protein was obtained with recovery of nearly 1%. About 222 times purification was achieved. Sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE) resolved two bands of acid phosphatase corresponding to molecular weight of 29 kilo Dalton (kDa) and 18 kDa. The molecular weights of native enzyme determined by gel filtration on calibrated Sephadex G-100 column were found to be 29 kDa and 18 kDa The apparent Km value of 29 kDa isoenzyme with p-nitrophenyl phosphate (pNPP) as substrate was 0.3 mM and Vmax was 1336 nmol.sec -1 .mg -1 of protein. The optimal pH for this enzyme was 5.5 and pH stability was 4-7. It had optimum temperature of 50 o

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Available abstract

of protein was obtained with recovery of nearly 1%. About 222 times purification was achieved. Sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE) resolved two bands of acid phosphatase corresponding to molecular weight of 29 kilo Dalton (kDa) and 18 kDa. The molecular weights of native enzyme determined by gel filtration on calibrated Sephadex G-100 column were found to be 29 kDa and 18 kDa The apparent Km value of 29 kDa isoenzyme with p-nitrophenyl phosphate (pNPP) as substrate was 0.3 mM and Vmax was 1336 nmol.sec -1 .mg -1 of protein. The optimal pH for this enzyme was 5.5 and pH stability was 4-7. It had optimum temperature of 50 o

Key concepts: Sephadex, Size-exclusion chromatography, Polyacrylamide gel electrophoresis, Molecular mass, Chromatography, Chemistry, Acid phosphatase, Enzyme

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Isolation, Purification and Characterization of Acid Phosphatase from Germinating Vigna radiata Seeds — Research Paper | ScholarLens