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Institute for Biological Chemistry and Nutrition, University of Hohenheim, D-7000 Stuttgart, West Germany
For the first time, in vivo utilization of two highly soluble and stable cystine-containing synthetic short-chain peptides, bis-L-alanyl-L-cystine and bis-glycyl-L-cystine, were investigated in adult rats. Within 5 min after an intravenous bolus, blood samples were drawn (inferior vena cava) and plasma amino acid and peptide levels were determined using RP-HPLC (precolumn derivatization with 5-dimethylaminonaphthalene-1-sulfonylchloride). Both peptides were rapidly cleared from plasma (estimated elimination t1/2:4 min for the glycyl peptide and less than 2 min for the alanyl peptide). The initial high amounts of mono-L-alanyl-L-cystine and mono-glycyl-L-cystine as well as the prompt increase of the constituent free amino acids alanine, glycine and cystine strongly suggest that the peptide disappearance is mainly due to a very fast two-step hydrolysis in the extracellular compartment, presumably catalyzed by soluble and/or plasma membrane-bound peptidases. The observed rapid hydrolysis may serve as first evidence that short-chain peptides with C-terminal cystine residue may represent efficient sources of free cystine in parenteral nutrition.
KEY WORDS: cystine peptides in vivo utilization parenteral nutrition
1 This study was supported by grants from BMWi (Industrielle Gemeinschaftsforschung, AIF No. 6668) and Pfrimmer and Company, Erlangen, FRG.
2 Present address: ICI Pharma, Plankstadt, FRG.
Manuscript received 19 April 1988. Revision accepted 8 July 1988.