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Reagent stability in Rosen's ninhydrin method of analysis for amino acids

1963; Elsevier BV; Volume: 6; Issue: 1 Linguagem: Inglês

10.1016/0003-2697(63)90013-7

1096-0309

D.R. Grant,

Various Chemistry Research Topics

The adsorption and binding of amino acids (aspartic acid, cysteine, glycine, proline and arginine), ranging in molecular weight from 115 to 174 and in isoelectric point from pH 2.8 to 10.8, to montmorillonite [M] and kaolinite [K] homoionic to H, Na, Ca, Zn, La or Al were studied in unbuffered suspensions. Aspartic acid was adsorbed and bound on M homoionic to Ca or Zn but only adsorbed to K homoionic to Ca or Zn. Cysteine was only adsorbed on M homoionic to Al and adsorbed and bound on M homoionic to Zn and on K homoionic to H or Zn. Proline was adsorbed and bound on M homoionic to H, Ca or Zn and on K homoionic to H; it was adsorbed but not bound on both M and K homoionic to Al. Arginine was adsorbed and bound on M homoionic to H or Al and only adsorbed on K homoionic to Ca or Zn. Glycine was not bound on any of the clays. The amounts of amino acid adsorbed and bound (measured by the loss of amino acid from solution) and the class (Giles et al., 1974a and b) of both the adsorption and binding isotherms (retention against ultimate washing with water) were dependent on the type of amino acid, the type of clay, the type of cation predominant on the clays and the basicity or the additional function moiety (e.g. carboxyl, thiol, guanido) of the amino acid. The relative values of the non-standard free energy of clay-amino acid complexes that had isotherms of the Giles C-class were dependent on the type and molecular weight of the amino acid and on the exchangeable cation on the clay.