1. This paper reports an investigation of whether the dipeptides glycylsarcosine and l-lysyl-l-lysine share a single mediated transport mechanism into hamster jejunum, or whether one of these peptides is taken up in part by a mediated mechanism unavailable to the other. The investigation, using rings of everted jejunum in vitro, was carried out at pH 5 in order to reduce brush border and/or intramedium hydrolysis of lysyl-lysine.

2. The kinetics of uptake of each peptide was studied over a wide range of concentrations. Estimates of the simple diffusion component in uptake of each peptide were made by the method of self-inhibition of transport as previously described. After correction for simple diffusion, uptake of each peptide conformed to Michaelis-Menten kinetics, and values for Kt and Vmax. were obtained.

3. It was found that each peptide was capable, at infinitely high concentration, of complete inhibition of mediated uptake of the other. The inhibitory effect was competitive. We concluded that glycylsarcosine and lysyl-lysine were taken up by a common mediated mechanism (or possibly mechanisms), neither peptide being taken up by a mediated mechanism unavailable to the other.

4. A previous paper showed that l-glutamyl-l-glutamic acid and glycylsarcosine were taken up by a common mediated mechanism, and this paper shows that l-lysyl-l-lysine and glycylsarcosine are taken up by a common mediated mechanism. It is therefore postulated that the neutral dipeptide glycylsarcosine, the acidic dipeptide glutamyl-glutamic acid and the basic dipeptide lysyl-lysine all share a common mediated mechanism for uptake. This suggests that peptide uptake differs from amino acid uptake in that it is indifferent to the net charge on the amino acid side chain(s).

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