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L. and Schelstraete, M. (1989) The estimation of ‘available lysine’ in human foods by three chemical procedures. Plant Foods for Human Nutrition 39, 12–135. , Gatta, M. I. (2000) Amperometric determination of underivatized amino acids at a nickel-modified gold electrode by anion-exchange chromatography. Journal of Chromatography A 878, 57–67. , Hernandez, T. and Hernandez, A. (1997) An isocratic high-performance liquid chromatographic method for determining the available lysine in foods. Journal of Chromatographic Science 35, 423–429.

1996) optimized the reaction conditions of guanidination in casein and soybean meal. They achieved 100% lysine conversion for the soluble milk protein and just under 80% for soy. These authors, like Ravindran et al. (1996), were interested in the preparative guanidination of feedstuff to determine endogenous amino acid secretions in digestibility trials. The latter studies focused mainly on optimal conversion in cottonseed protein, where up to 64% of the lysine was converted into homoarginine, and conversion rates of other feed raw materials are also given.

Zeitschrift für Tierphysiologie, Tierernährung und Futtermittelkunde 63, 188–197. , Reichel, A. and Ermisch, A. (1994) Simple high-performance liquid-chromatographic analysis of free primary amino-acid concentrations in rat plasma and cisternal cerebrospinal fluid. Journal of Chromatography B 657, 185–191. D. M. (1996) Chemiluminescent nitrogen detection as a new technique for purity assessment of synthetic peptides separated by reversed-phase HPLC. Peptide Research 9, 40–44. -C. , Venuat, M. and Jackson, D.

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