Biochemical Characterization of Amandin, the Major Storage Protein in Almond (Prunus dulcis L.)
| Autor: | Kenneth H. Roux, Mahesh Venkatachalam, Suzanne S. Teuber, K. W. C. Sze-Tao, Shridhar K. Sathe, Walter J. Wolf |
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| Rok vydání: | 2002 |
| Předmět: |
Chemical Phenomena
Chemical Precipitation Legumin Storage protein Amino Acid Sequence Amino Acids Threonine Chromatography High Pressure Liquid Plant Proteins chemistry.chemical_classification Chromatography Molecular mass Chemistry Physical Isoelectric focusing General Chemistry Amino acid Molecular Weight Freeze Drying Isoelectric point chemistry Biochemistry Plant protein Chromatography Gel Electrophoresis Polyacrylamide Gel Prunus Isoelectric Focusing Peptides General Agricultural and Biological Sciences |
| Zdroj: | Journal of Agricultural and Food Chemistry. 50:4333-4341 |
| ISSN: | 1520-5118 0021-8561 |
| DOI: | 10.1021/jf020007v |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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