Content:
Chapter 1 dietary and Metabolic features of Peptide shipping (pages 1–10): R. F. Crampton
Chapter 2 Peptide delivery in micro organism (pages 11–16): Charles Gilvarg
Chapter three Mechanisms of Bacterial Peptide shipping (pages 17–42): J. W. Payne
Chapter four Peptidase task and Peptide Metabolism in Escherichia coli (pages 43–57): Sofia Simmonds
Chapter five Peptide delivery via Mammalian intestine (pages 49–70): D. H. Smyth
Chapter 6 premiums of Peptide Uptake by way of Small gut (pages 71–92): D. M. Matthews
Chapter 7 Peptides in Genetic mistakes of Amino Acid delivery (pages 93–106): M. D. Milne
Chapter eight Subcellular Fractionation of the Enterocyte with exact connection with Peptide Hydrolases (pages 107–122): T. J. Peters
Chapter nine Membrane Digestion and Peptide delivery (pages 123–143): A. M. Ugolev

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Extra info for Ciba Foundation Symposium 4 - Peptide Transport in Bacteria and Mammalian Gut

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And F. M. RICHARDS (1968) J. Mol. Biol. 33,795-807. PETERS, V. , J. M. PRESCOTT and E. E. SNELL (1953) J. Biol. Chem. 202,521-532. PIPERNO, J. R. and D. L. OXENDER (1968) J. Biol. Chem. 243, 5914-5920. PIITMAN, K. , S. LAKSHMANAN and M. P. BRYANT (1967) J. Bacteriol. 93, 1499-1508. SHANKMAN, S . , V. GOLD,S. HIGAand R. SQUIRES (1962) Biochem. Biophys. Res. 9, 25-3 1. SIMMONDS, S. (1966) J. Biol. Chem. 241,2502-2508. SIMMONDS, S . and J. S. FRUTON (1948) J. Biol. Chem. 174,705-715. SIMMONDS, S .

Payne: Christensen (1963) concluded that Schiff base formation was not involved in the uptake of amino acids in mammalian cells. In my paper I was merely suggesting one possible mechanism compatible with the requirement for the N-terminal a-amino group, but to see whether there is any substance in the speculation one must first carry out experiments of the type that I suggested. At the same time as our work on the N-methylated (sarcosyl) peptides we also studied prolyl peptides (Payne 1971b), and concluded that these iminopeptides could also use the normal peptide transport systems in E.

Preliminary data suggest that the aminopeptidase may be a metallo-enzyme, but no preparation exhibiting an absolute requirement for a metal ion has been obtained. However, with undialysed preparations approximately equal activity (substrate, leucylleucine) is seen in the presence of 25 to + Peptidases in E. coli 47 1350 pM-Mn2+, but supplementation of 25 pM-Mn2+ with 1300 p ~ - C o ~or+ Zn2 causes significant inhibition. Although all the aminopeptidase activity of soluble fraction P towards X-leucylglycine tripeptides is recovered in the AP subfraction, the low activity of AP towards X-glycylglycine and X-glycyl-X (where X is methionyl or leucyl) accounts for no more than about 25 % of the activity of soluble fraction P towards such substrates.

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