Biochemical characterization of amandin,the major storage protein in almond (Prunus dulcis L.) |
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Authors: | Sathe Shridhar K Wolf Walter J Roux Kenneth H Teuber Suzanne S Venkatachalam Mahesh Sze-Tao Kar Wai Clara |
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Institution: | Department of Nutrition, Food and Exercise Sciences, Florida State University, Tallahassee, Florida 32306-1493, USA. ssathe@mailer.fsu.edu |
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Abstract: | The almond major storage protein, amandin, was prepared by column chromatography (amandin-1), cryoprecipitation (amandin-2), and isoelectric precipitation (amandin-3) methods. Amandin is a legumin type protein characterized by a sedimentation value of 14S. Amandin is composed of two major types of polypeptides with estimated molecular weights of 42-46 and 20-22 kDa linked via disulfide bonds. Several additional minor polypeptides were also present in amandin. Amandin is a storage protein with an estimated molecular weight of 427,300 +/- 47,600 Da (n = 7) and a Stokes radius of 65.88 +/- 3.21 A (n = 7). Amandin is not a glycoprotein. Amandin-1, amandin-2, and amandin-3 are antigenically related and have similar biochemical properties. Amandin-3 is more negatively charged than either amandin-1 or amandin-2. Methionine is the first essential limiting amino acid in amandin followed by lysine and threonine. |
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