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Proteins in Relation to Vigor and Viability of White Lupin (Lupinus albus L.) Seed Stored for 26 Years

The aim of the study was to evaluate the vigor and viability as well as to determine and compare the contents of selected protein fractions of white lupin (Lupinus albus L.) seeds stored for 26 years at temperatures of -14°C and +20°C. The seeds stored at -14°C germinated in 86.3%, while the seeds s...

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Autores principales: Dobiesz, Malwina, Piotrowicz-Cieślak, Agnieszka I.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Frontiers Media S.A. 2017
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5554512/
https://www.ncbi.nlm.nih.gov/pubmed/28848591
http://dx.doi.org/10.3389/fpls.2017.01392
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author Dobiesz, Malwina
Piotrowicz-Cieślak, Agnieszka I.
author_facet Dobiesz, Malwina
Piotrowicz-Cieślak, Agnieszka I.
author_sort Dobiesz, Malwina
collection PubMed
description The aim of the study was to evaluate the vigor and viability as well as to determine and compare the contents of selected protein fractions of white lupin (Lupinus albus L.) seeds stored for 26 years at temperatures of -14°C and +20°C. The seeds stored at -14°C germinated in 86.3%, while the seeds stored at +20°C did not germinate at all. The viability evaluation was confirmed by the measuring electroconductivity of seed exudates. In seeds stored at -14°C the contents of γ, δ, and β conglutin were 14, 4 and 69 mg g(-1) fresh mass, respectively, while in seed stored at +20°C they were 15.5, 3, 65 mg g(-1) fresh mass, respectively. One-dimensional electrophoresis of γ and δ conglutin fractions indicated the presence of several intense polypeptide bands with molecular weights from 23.0 to 10.3 kDa. Polypeptide bands with a molecular weight of 22.4 and 19.8 kDa exhibited almost two times higher expression in the seeds stored at -14°C compared to the seeds stored at +20°C. Electrophoresis revealed 310 protein spots on the maps generated for seeds stored at -14°C, and 228 spots for seeds stored at +20°C. In seeds stored at +20°C most polypeptide subunits had a pI ranging from 4.5 to 7 and a molecular weight of 10–97 kDa. The greatest differences in the contents of polypeptides between the analyzed variants was observed within the range of 20–45 kDa (-14°C: 175, +20°C: 115 protein spots) and within the range of 65–97 kDa (-14°C: 103, +20°C: 75 protein spots). In seeds stored at +20°C, a clear decline in basic (8–10 pI) polypeptides was observed. The study demonstrated that the polypeptides identified as γ and δ conglutins are probably closely related to vigor and viability of seeds.
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spelling pubmed-55545122017-08-28 Proteins in Relation to Vigor and Viability of White Lupin (Lupinus albus L.) Seed Stored for 26 Years Dobiesz, Malwina Piotrowicz-Cieślak, Agnieszka I. Front Plant Sci Plant Science The aim of the study was to evaluate the vigor and viability as well as to determine and compare the contents of selected protein fractions of white lupin (Lupinus albus L.) seeds stored for 26 years at temperatures of -14°C and +20°C. The seeds stored at -14°C germinated in 86.3%, while the seeds stored at +20°C did not germinate at all. The viability evaluation was confirmed by the measuring electroconductivity of seed exudates. In seeds stored at -14°C the contents of γ, δ, and β conglutin were 14, 4 and 69 mg g(-1) fresh mass, respectively, while in seed stored at +20°C they were 15.5, 3, 65 mg g(-1) fresh mass, respectively. One-dimensional electrophoresis of γ and δ conglutin fractions indicated the presence of several intense polypeptide bands with molecular weights from 23.0 to 10.3 kDa. Polypeptide bands with a molecular weight of 22.4 and 19.8 kDa exhibited almost two times higher expression in the seeds stored at -14°C compared to the seeds stored at +20°C. Electrophoresis revealed 310 protein spots on the maps generated for seeds stored at -14°C, and 228 spots for seeds stored at +20°C. In seeds stored at +20°C most polypeptide subunits had a pI ranging from 4.5 to 7 and a molecular weight of 10–97 kDa. The greatest differences in the contents of polypeptides between the analyzed variants was observed within the range of 20–45 kDa (-14°C: 175, +20°C: 115 protein spots) and within the range of 65–97 kDa (-14°C: 103, +20°C: 75 protein spots). In seeds stored at +20°C, a clear decline in basic (8–10 pI) polypeptides was observed. The study demonstrated that the polypeptides identified as γ and δ conglutins are probably closely related to vigor and viability of seeds. Frontiers Media S.A. 2017-08-11 /pmc/articles/PMC5554512/ /pubmed/28848591 http://dx.doi.org/10.3389/fpls.2017.01392 Text en Copyright © 2017 Dobiesz and Piotrowicz-Cieślak. http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.
spellingShingle Plant Science
Dobiesz, Malwina
Piotrowicz-Cieślak, Agnieszka I.
Proteins in Relation to Vigor and Viability of White Lupin (Lupinus albus L.) Seed Stored for 26 Years
title Proteins in Relation to Vigor and Viability of White Lupin (Lupinus albus L.) Seed Stored for 26 Years
title_full Proteins in Relation to Vigor and Viability of White Lupin (Lupinus albus L.) Seed Stored for 26 Years
title_fullStr Proteins in Relation to Vigor and Viability of White Lupin (Lupinus albus L.) Seed Stored for 26 Years
title_full_unstemmed Proteins in Relation to Vigor and Viability of White Lupin (Lupinus albus L.) Seed Stored for 26 Years
title_short Proteins in Relation to Vigor and Viability of White Lupin (Lupinus albus L.) Seed Stored for 26 Years
title_sort proteins in relation to vigor and viability of white lupin (lupinus albus l.) seed stored for 26 years
topic Plant Science
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5554512/
https://www.ncbi.nlm.nih.gov/pubmed/28848591
http://dx.doi.org/10.3389/fpls.2017.01392
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