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Studies on the protein in soybean hypocotyl

1958; Elsevier BV; Volume: 78; Issue: 1 Linguagem: Inglês

10.1016/0003-9861(58)90326-6

1096-0384

J. J. Rackis, A. K. Smith, Hènry A. Sasame,

Phytoestrogen effects and research

Abstract Two methods for separation of soybean hypocotyl are described. Solubility data are presented for the nitrogen constituents of hypocotyl extracts. Experiments indicate that removal of phytic acid is responsible for the shift in the pH of minimum solubility of hypocotyl proteins to higher values. Electrophoretic studies indicate that the interaction of phytic acid with components of the acid-precipitated protein greatly modifies its electrophoretic behavior; the major component, when phytate-free, contains two electrophoretically distinct proteins. Ultracentrifugal studies at pH 7.6 show the presence of three resolvable fractions having s 20 values of 2 S , 5 S , and 10 S , and at pH 3.0 two resolvable fractions having s 20 values of 2 S and 6 S . A comparison of the solubility and of the electrophoretic and ultracentrifugal properties of acid-precipitated proteins of the hypocotyl and cotyledon has disclosed similar as well as different properties.