Abstract
The seed storage proteins of
Pisum
(pea) and
Phaseolus vulgaris
(French bean) exhibit genetic variation for polypeptide structure; genetical studies indicate that most of the major storage protein genes exhibit simple, codominant Mendelian inheritance. Biochemical analysis of the storage protein polypeptides and their messenger RNAs shows that the allelic alternatives are probably small families of closely linked structural genes. Two of these genes - those for the major legumin gene family and for convicilin, both from
Pisum sativum
- have been assigned to specific sites on linkage groups. Genes affecting the synthesis of legumin in
Pisum sativum
and of phaseolin in
Phaseolus vulgaris
have been identified.
Subject
Industrial and Manufacturing Engineering,General Agricultural and Biological Sciences,General Business, Management and Accounting,Materials Science (miscellaneous),Business and International Management
Reference90 articles.
1. Badley R. E. Atkinson D. Hauser H. Oldani D. Green J. P. & Stubbs J. M. 1975 The structure physical and chemical properties of the soybean protein glycinin. Biochim. biophys. 412 214-228.
2. Bailey C. J. & Boulter D. 1971 Urease a typical seed protein of the Leguminosae. In Chemotaxonomy of the Leguminosae(ed. J. B. Harborne D. Boulter & B. L. Turner) pp. 485-502. London and New York: Academic
3. Press.
4. The biosynthesis and processing of high molecular weight precursors ofsoybean glycinin subunits. J. biol;Barton K. A.;Chem.,1982
5. Identification of Cultivar Differences in Seed Polypeptide Composition of Peanuts (Arachis hypogaea L.) by Two-Dimensional Polyacrylamide Gel Electrophoresis
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