@article { author = {Gonnety, Jean Tia and Niamke, Sebastien and Meuwiah Faulet, Betty and N’guessan Kouadio, Eugène Jean-Parfait and Patrice Kouame, Lucien}, title = {Purification and characterization of two acid phosphatases from germinating peanut (Arachis hypogaea) seed}, journal = {Iranian Journal of Biotechnology}, volume = {4}, number = {1}, pages = {26-35}, year = {2003}, publisher = {National Institute of Genetic Engineering and Biotechnology of Iran}, issn = {1728-3043}, eissn = {2322-2921}, doi = {}, abstract = {The maximum acid phosphatasic activity was detected in peanut seed at the 5th day of germination. At least, two acid phosphatases were purified by successive chromatography separations on DEAE-Sepharose CL-6B, CM-Sepharose CL-6B, Sephacryl S-100 HR, and Phenyl-Sepharose HP to apparent homogeneity from five days old cotyledon of peanut after germination. These isoenzymes, designated peanut cotyledon acid phosphatase 1 and 2 (PCAP 1 and PCAP 2), had native molecular weights of approximately 27.5 and 24 kDa by gel permeation, respectively. SDS-PAGE (Sodium Dodecyl Sulfate Polyacrylamide Gel Electrophoresis)of PCAP 1 and PCAP 2 resolved a single protein band (each) that migrated to approximately 27 and 29 kDa,respectively. Thus, these acid phosphatases likely function as a monomer. The two isoenzymes had a similar optimum temperature (55°C), two closely optima pH (5.6 and 5.0), and appeared to be stable in the presence of some detergents such as Triton X-100, Nonidet P-40, Taurocholic acid sodium salt, Polyoxyethylene-9-lauryl ether as well as Mg2+, Sr2+,Fe3+ and Ba2+. Substrate specificity indicated that PCAP 1 and PCAP 2 hydrolyzed a broad range of phosphorylated substrates. However, natural substrates such as ADP, ATPand phenylphosphate had the highest rate of hydrolysis for the two isoenzymes.}, keywords = {Acid Phosphatase,Arachis hypogaea,Cotyledon,Germination,Peanut}, url = {https://www.ijbiotech.com/article_6977.html}, eprint = {https://www.ijbiotech.com/article_6977_cdd963f4077e68f8a04e7a45b8a19b14.pdf} }