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A study was made on the use of an amino acid analyzer for determining lysinoalanine (LAL) in food proteins. Protein bound lysinoalanine is liberated by acid hydrolysis, separated on a high pressure cation exchange column with a sodium citrate buffer (0.35N sodium; pH 5.30), and detected calorimetrically after reaction with ninhydrin. The procedure is sensitive to concentrations of 50 pg LAL/g sample and concentrations as low as 20 μg/g sample have been detected. Application to food products, problems encountered, and the use of two different column temperatures (52 and 65°C) for different products to achieve better separation are described.
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Marvin L. Raymond (1980) studied this question.
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