Abstract
Acid phosphatase from mung bean (Vigna radiata) germinated seeds was partially purified via ammonium sulfate precipitation and fully purified via gel excision and heat denaturation, yielding a 29 kDa protein. Using 4-nitrophenylphosphate as a substrate, Vmax and Km values of 0.10 µmol/min and 0.27 mM, respectively, were obtained. The acid phosphatase was heat resistant, enhanced by the presence of Fe2+ and Mn2+ salts, and inhibited by the presence of citrate. Mung bean acid phosphatase reacted immunologically with primary antibodies against Solanum tuberosum acid phosphatase, while polymerase chain reaction (PCR) analyses suggest there are some common sequences between mung bean acid phosphatase DNA and that of Arabidopsis thaliana acid phosphatase vegetative storage protein. This suggests plant acid phosphatases are structurally as well as functionally related. Key words: Acid phosphatase, mung bean, Vigna radiata, vegetative storage protein.
Highlights
Phosphatases (3.1.3) are a diverse group of enzymes found in most living systems
Following the protocol outlined in Surchandra et al (2012), ammonium sulfate was used in a two-step process to partially purify acid phosphatase (AP) in order to precipitate and concentrate the protein
For purposes of keeping to the Surchandra et al (2012) protocol for comparisons, most data reported in this paper involve the two step ammonium sulfate precipitation with a final ammonium sulfate cut of 70%
Summary
Phosphatases (3.1.3) are a diverse group of enzymes found in most living systems. Historically, they have been less well studied than protein kinases, but recently there has been more interest in both protein and genetic characterization and regulation (Bheri et al, 2021; Schweighofer and Meskiene, 2015; Brautigan, 2013; Uhrig et al, 2013; Anand and Srivastava, 2012; Moorman and Brayton, 2021). Phosphatases appear to have the important roles of liberating and securing phosphates for growth, especially in germinating seeds (Duff et al, 1994; Anand and Srivastava, 2012). These enzymes are abundant and robust enough that their extraction and analyses are routinely used as a laboratory experiment in undergraduate biochemistry courses (Moorman and Brayton, 2021) as done in Northern Michigan University.
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