PASTIC Dspace Repository

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

Show simple item record

dc.contributor.author SADIA NADIR
dc.contributor.author ASMA SAEED
dc.contributor.author RUBINA NAZ
dc.contributor.author AISHA SIDDIQUA
dc.contributor.author MEHRIN SHERAZI
dc.contributor.author SULTAN MEHMOOD WAZIR
dc.contributor.author AHMAD SAEED
dc.date.accessioned 2023-12-20T04:39:03Z
dc.date.available 2023-12-20T04:39:03Z
dc.date.issued 2012-06-20
dc.identifier.citation Nadir, S., Saeed, A., Naz, R., Siddiqua, A., Sherazi, M., Wazir, S. M., & Saeed, A. (2012). Isolation, purification and characterization of acid phosphatase from germinating Vigna radiata seeds. Journal of the Chemical Society of Pakistan, 34(3). en_US
dc.identifier.issn 0253-5106
dc.identifier.uri http://142.54.178.187:9060/xmlui/handle/123456789/20031
dc.description.abstract The acid phosphatase (EC 3.1.3.2 ) has been purified from germinating seeds of vigna radiata through ammonium sulphate precipitation, DEAE-Cellulose chromatography and concanavalin A-Sepharose 4B chromatography. The specific activity of 1291 nkat.mg⁻¹of 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 50oC and temperature stability was 0- 50oC. The enzyme hydrolysed various phosphorylated compounds non-specifically. It was competitively inhibited by phosphate, vanadate while fluoride showed non- competitive inhibition and molybdate exhibited an inhibition of mixed type. It was found insensitive to tartrate and concluded that this enzyme was recognized as tartrate resistant acid phosphatase. en_US
dc.description.sponsorship The chemical society of Pakistan is an approved society from the PSF. en_US
dc.language.iso en en_US
dc.publisher HEJ Research Institute of Chemistry, University of Karachi, Karachi. en_US
dc.subject Acid phosphatase en_US
dc.subject Vigna radiata en_US
dc.subject purification; characterization en_US
dc.subject seedlings; isoenzyme en_US
dc.title Isolation, Purification and Characterization of Acid Phosphatase from Germinating Vigna radiata Seeds. en_US
dc.type Article en_US


Files in this item

This item appears in the following Collection(s)

Show simple item record

Search DSpace


Advanced Search

Browse

My Account