PMID: 8580776Jan 1, 1996Paper

Characterisation of a developmentally related polypeptide with glutelin solubility characteristics from Lupinus albus L

Planta
J CostaC P Ricardo

Abstract

Proteins from Lupinus albus L. cv. Rio Maior seeds were fractionated according to solubility criteria. Patterns of concanavalin A (ConA)-binding polypeptides from the different classes, albumins, globulins, glutelins and prolamins, were established by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Two bands of apparent molecular masses of 29 and 23.5 kDa with glutelin solubility characteristics bound the lectin. The 23.5-kDa band was separated by two-dimensional electrophoresis into two components: one glycosylated and heterogeneous with an isoelectric point of approx. 10 (designated as G23) and another, not detected with ConA, precipitating in the first dimension. The amino acid and hexosamine analysis of G23 showed that it is particularly rich in Gly (11.2%), Glx (10.0%), Ser (9.0%), Leu (8.2%), Asx (7.5%), and Pro (6.7%) and that it has a considerable content of the sulphur-containing amino acids Met (2.0%) and Cys (5.8%) and contains glucosamine. The determined N-terminal amino acid sequence of G23 was: 1KG(R)V5KGTGD10(T)PXXV15XLY(N)R20T, and this had no significant similarity to any of the amino acid sequences contained in the data bank SWISS-PROT 26. The glycoprotein G23 was completely deglycosylated with pept...Continue Reading

Citations

Feb 13, 2010·Journal of the American Chemical Society·Erica L CampbellDale L Boger
Aug 31, 2011·Journal of Natural Products·K Brian KilldayMichael S Tempesta
Oct 2, 2002·Physiologia Plantarum·Allison E. McDonaldGreg C. Vanlerberghe
Apr 1, 1997·Proceedings of the National Academy of Sciences of the United States of America·S GutierresR De Paepe
Feb 14, 1997·The Journal of Biological Chemistry·S Y Mir-ShekariI T Schulze

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