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Precursors of storage proteins in Lupinus angustifolius
journal contribution
posted on 1984-07-15, 00:00 authored by K R Gayler, B G Boadle, M Snook, Liz JohnsonLiz JohnsonThe proteins that are synthesized during differentiation and development in the cotyledons of Lupinus angustifolius L. were characterized both in situ and after purification. The proteins present in situ were separated by sodium dodecyl sulphate/polyacrylamide-gel electrophoresis and subjected to 'Western'-blot analysis to identify immunologically related polypeptides. The major storage proteins of the lupin, conglutins a and /, were both present in juvenile tissue only as higher M, precursors. For conglutin /, a family of at least three polypeptides of Mr 66000-72000
accumulated during the earliest phases of protein synthesis in the developing cotyledon (20-28 days after flowering). Later in development each of these polypeptides disappeared and there was the concurrent appearance in the cotyledon of the lower-Mr fragments characteristic of mature conglutin P. For conglutin a, an equivalent family of precursor polypeptides of M, 60000-83000 was detected. Multiple internal sites for proteolytic cleavage of all these precursors appeared to be present. However, processing of the precursors was sufficiently slow to allow them to accumulate to over 50% of total soluble protein in juvenile tissue. The precursors were purified by column chromatography under non-dissociating conditions and shown by ultracentrifugation to be multimeric proteins with Mr values in the range 150000-200000.
accumulated during the earliest phases of protein synthesis in the developing cotyledon (20-28 days after flowering). Later in development each of these polypeptides disappeared and there was the concurrent appearance in the cotyledon of the lower-Mr fragments characteristic of mature conglutin P. For conglutin a, an equivalent family of precursor polypeptides of M, 60000-83000 was detected. Multiple internal sites for proteolytic cleavage of all these precursors appeared to be present. However, processing of the precursors was sufficiently slow to allow them to accumulate to over 50% of total soluble protein in juvenile tissue. The precursors were purified by column chromatography under non-dissociating conditions and shown by ultracentrifugation to be multimeric proteins with Mr values in the range 150000-200000.
History
Journal
Biochemical journalVolume
221Issue
2Pagination
333 - 341Publisher
Portland Press Ltd.Location
London, Eng.Publisher DOI
ISSN
0264-6021eISSN
1470-8728Language
enPublication classification
C1.1 Refereed article in a scholarly journalCopyright notice
1984, London: The Biochemical SocietyUsage metrics
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