Pyridoxal 5'-phosphate (PLP) is a B(6) vitamer acting as an agitator cofactor in assorted reactions of aminoacid metabolism and inhibiting glycation of biomolecules. Nonenzymatic glycation of aminophospholipids alters the adherence of lipid bilayers and corpuscle action as a result. Similarly to protein glycation, aminophospholipid glycation initially involves the accumulation of a Schiff base. In this work, we advised the accumulation of Schiff bases amid PLP and two compounds artful the arctic arch of accustomed aminophospholipids, namely: O-phosphorylethanolamine and O-phospho-D,L-serine. Based on the results, the pH-dependence of the diminutive constants of the two PLP-aminophosphate systems advised is identical with that for PLP-aminoacid systems. However, the amount and calm accumulation constants for the Schiff bases of the aminophosphates are low about to those for the aminoacids. A abstract abstraction by body anatomic approach of the accumulation apparatus for the Schiff bases of PLP with the two aminophospholipid analogues accepted that the activation activity of accumulation of the Schiff bases is greater with aminophosphates; on the added hand, that of hydrolysis is about agnate with aminoacids and aminophosphates.