Download Advances in Microbial Physiology, Vol. 36 by A.H. Rose, D.W. Tempest (Ed.) PDF

By A.H. Rose, D.W. Tempest (Ed.)

From the experiences of earlier Volumes "This sequence has continuously offered a well-balanced account of development in microbial physiology...Invaluable for instructing purposes." -AMERICAN SCIENTIST

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Extra resources for Advances in Microbial Physiology, Vol. 36

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Subsequent studies have endorsed this conclusion and have increasingly highlighted similarities between the systems present in various species. Many fastidious organisms utilize peptides as sources of essential amino acids and this has proved a useful means by which to study transport; commonly, peptides prove to be nutritionally more effective than corresponding mixtures of amino acids. , 1982 and Section XI). Inhibition requires that smugglins be accumulated intact and hydrolysed by intracellular enzymes; thus, sensitivity provides prima facie evidence for peptide transport.

1992). The p l value of the protein from E. , 1986). 55 respectively; each of these species yields the same single band on a sodium dodecylsulphatepolyacrylamide gel and has an identical N-terminal sequence. The apparent variation in OppA is also seen during its purification. Thus, when it is isolated on ion-exchange columns (Pharmacia FPLC MonoQ and Monos columns), it elutes as several poorly-resolved peaks, each of which converts to a single, sharp peak when again separated on a reverse-phase column (see above).

PAYNE AND M. W. SMITH side-chains of Lys3, but would be unaffected by smaller, neutral residues on other substrates. With small peptides, lacking an extended secondary structure, one domain of the binding protein might bind the peptide backbone predominantly, while another domain might interact with side chains on the substrate. Thus, the fluorescence results of Guyer et al. (1986) can be explained without the need to invoke two binding sites. A final point is the mutational loss of triornithine sensitivity with retention of growth using proline-containing peptides in certain oppA mutants.

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