Purification and Characterization of Two Acid Phosphatases from Germinating Peanut (Arachis hypogaea) Seed

نویسندگان: ثبت نشده
چکیده مقاله:

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.

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عنوان ژورنال

دوره 4  شماره 1

صفحات  26- 35

تاریخ انتشار 2003-10-01

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