Fractionation and partial characterization of tepary bean (Phaseolus acutifolius) proteins
1994
Idouraine, A. | Yensen, S.B. | Weber, C.W.
Tepary bean (Phaseolus acutifolius) proteins were fractionated sequentially according to solubility in sodium phosphate buffer (SPB), sodium chloride (salt), ethanol, 2-mercaptoethanol (2-ME), and sodium dodecyl sulfate (SDS) solutions, and characterized. The SPB protein fraction was significantly (P < 0.05) the highest (83.2% of the recovered protein) followed by salt protein fraction (13.7%, 2-ME (1.5%) ethanol (0.8%), and SDS (0.8%) protein fractions. The amino acid compositions of SPB, salt, ethanol, and 2-ME protein fractions were not significantly different. Methionine and cysteine concentrations were low in all fractions. The ethanol protein fraction had a significantly (P < 0.05) higher cysteine content (1.5%) than 2-ME (0.95%), salt (0.2%) or SPB (trace) protein fractions. SDS-PAGE of SPB and salt protein fractions contained 37 and 27 polypeptides, respectively, with major bands at 29, 45, and 49 kDa. Ethanol and SDS protein fractions had only a limited number of small polypeptides.
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