Special peptides

  • S. G. Waley
Part of the Handbuch der Pflanzenphysiologie / Encyclopedia of Plant Physiology book series (532, volume 8)


The study of peptides in plants has been dominated by two aims. Most of the work described here has been carried out in order to identify some “active principle”, which has turned out to contain peptide bonds. Such “principles” may be active towards bacteria (e.g. gramicidin, penicillin, etc.), plants (e.g. lycomarasmin) or animals (e.g. the ergot alkaloids). The primary interest in much of this work has been to determine the structure of these physiologically active peptides; it is not generally known why they are active, nor the part they play in the metabolism of the organisms whence they originated. Chemically, these peptides are interesting in the variety of structures displayed and in the methods used to purify them and determine their structure; the use of these methods is a guide to the methods likely to be of promise in the purification and structure determination of proteins. Biologically, too, these physiologically active peptides serve as a reminder of the many possible complexities latent in the protein molecule. The second aim in the study of peptides is a more general one. Living cells commonly contain a score or so of amino-acids and many proteins, and the proteins themselves usually have at least 100 amino-acid residues in their molecules. Whether molecules of intermediate size are present (and if so, the part they play in protein metabolism) is an important, but largely unanswered, question. This section is written from the point of view that the main interest in the “active principle” type of work lies in the structure of the products, whereas the main interest at the moment in the second type of work lies in the analytical techniques. One of the most frequently used techniques is paper chromatography; its application to the study of the nitrogenous constituents of plants is described in a review by Steward and Thomson (1950).


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  • S. G. Waley

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