Preparative separation of an enzymatic hydrolysate of 14C-labelled proteins.
The preparative separation of an enzymatic hydrolysate by a step gradient of a lithium-sodium citrate buffer was studied. Using a two-column arrangement, 10 GBq of 14C-labelled enzymatic hydrolysate or 250 mg of inactive hydrolysate were separated within 36 h. After the chromatographic separation, the fractions of amino acids were isolated from the citrate eluents on weak cation exchangers with an ethylene glycol-poly(methyl methacrylate) matrix. The use of volatile organic acids as an eluent was possible due to the weak interactions with the cation matrix.
Kleinmann
I
I
Institute for Research, Production and Application of Radioisotopes, Prague, Czechoslovakia.
Svoboda
V
V
Vocková
J
J
D000596:Amino Acids / Q000032:analysis; D006868:Hydrolysis; D011492:Protein Hydrolysates / Q000032:analysis*
D000596:Amino Acids; D011492:Protein Hydrolysates