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Chemistry of legume protease inhibitors and their use in taxonomy

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Abstract

Protease inhibiting proteins, especially those that bind to trypsin and chymotrypsin, are widely distributed withinLeguminosae. Data on the primary structure and reactive sites known for some of them allow a classification into inhibitor families; inhibitors with the same topological molecular structures are grouped together. Evaluation of amino acid sequences based on amino acid replacements has been shown to be useful for understanding taxonomic and phylogenetic relations at the molecular level. The application of this method to theLeguminosae is demonstrated here with the example of the Bowman—Birk inhibitor family.

A rapid method of obtaining inhibitor patterns from seed extracts is the use of disc electrophoresis followed by specific staining of the inhibitor bands. The types of inhibitor patterns, in combination with trypsin and chymotrypsin inhibitor activities and the quotients of these two activities, can be used for taxonomic studies. Results obtained with this method were first proven to correlate with the results of other chemotaxonomic techniques within the genusAcacia. In the case of Australian acacias, this technique was used to demonstrate closer relationships between uninervedRacemosae andBotryocephalae (Bipinnatae) and also betweenPlurinerves andPulchellae (Bipinnatae) than between the twoBipinnatae and betweenPlurinerves andJuliflorae. This technique has also been used to excludeAcacia mitchellii from the seriesPulchellae.

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Authors and Affiliations

  1. Institut für Lebensmittelchemie, Technische Universität München, Lichtenbergstr, 4, D-8046, Garching, FRG

    Jürgen K. P. Weder

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  1. Jürgen K. P. Weder
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Held at the 75th Annual Meeting of the AOCS in Dallas, TX, April 29–May 3, 1984.

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Weder, J.K.P. Chemistry of legume protease inhibitors and their use in taxonomy. Plant Food Hum Nutr 35, 183–194 (1985). https://doi.org/10.1007/BF01092194

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