Lectins from Pisum arvense seeds behave differently from storage proteins during germination in the darkness

ABSTRACT - The mobilization of seed proteins from Pisum arvense L. during germination in the absence of light was studied. The seeds were found to be completely consumed 22 days after germination and seedlings ceased growth after the 18th day. SDS-PAGE indicated that the main protein bands correspond to high molecular mass storage proteins which undergo proteolysis in the initial stages of germination and are not detected after the 7th day of germination. However, the corresponding lectin profiles were detected during the entire germination process, suggesting that these proteins are strongly resistant to seed proteolytic enzymes and should be important for seedling establishment. Furthermore, haemagglutinating activity in cotyledons was detected until 22 days after germination, indicating that the lectins remain active even in senescent cotyledons.

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Taxonomic significance of seed protein profiles in Acacia, with special reference to Acacia emilioana

Australian Systematic Botany ◽

10.1071/sb01040 ◽

2003 ◽

Vol 16 (1) ◽

pp. 35 ◽

Cited By ~ 2

Author(s):

Alicia L. Lamarque ◽

Renée H. Fortunato

Keyword(s):

Seed Protein ◽

Seed Proteins ◽

High Concentration ◽

Protein Patterns ◽

Qualitative And Quantitative ◽

Sds Page ◽

Electrophoretic Data ◽

Main Protein ◽

Protein Components ◽

Total Seed

Total seed proteins of 10 Acacia species were examined by SDS–PAGE. The protein patterns showed qualitative and quantitative differences among the taxa analysed. The main protein components of most species examined had MW's in the range of 38.5–49.0 × 103. Subgenus Aculeiferum differed from subg. Acacia in the presence of a high concentration of proteins in the range of 20–24.5 × 103. Hierarchical clustering of the 10 taxa was undertaken, based on Jaccard distances calculated from electrophoretic data. The species grouped in two main clusters, representing the two subgenera of Acacia that occur in America, namely subg. Acacia and subg. Aculeiferum. The taxonomic placement of Acacia emilioana, a species with uncertain sectional affinity within subg. Aculeiferum, is discussed.

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Mobilization of seed storage proteins is crucial to high vigor in common bean seeds

Ciência Rural ◽

10.1590/0103-8478cr20200894 ◽

2022 ◽

Vol 52 (2) ◽

Author(s):

Natalia Carolina Moraes Ehrhardt-Brocardo ◽

Cileide Maria Medeiros Coelho

Keyword(s):

Storage Proteins ◽

Seed Proteins ◽

Seed Storage ◽

Seed Storage Proteins ◽

Seed Vigor ◽

Intensity Difference ◽

Biochemical Component ◽

Germination Process ◽

Radicle Protrusion ◽

Relationship Of

ABSTRACT: Seed germination is a complex process controlled by many factors, in which physical and biochemical mechanisms are involved and the mobilization of reserves is crucial for this process to occur. Although, seed reserve mobilization is usually thought to be a post-germination process, seed reserve proteins mobilization occurs during germination. This study quantified seed proteins of bean genotypes during different hydration times, in order to understand the process of protein mobilization and whether there is relationship of this biochemical component with seed vigor. This study was conducted using seeds with different levels of vigor, genotypes with highest (13, 42, 55 and 81) and lowest (07, 23, 44, 50, IPR-88-Uirapurú and Iapar 81) physiological quality. High vigor genotypes showed greater efficiency in hydrolysis and mobilization of protein component, because they presented low globulins content in cotyledons at radicle protrusion in relation to low vigor genotypes (07, 23 and 50). The protein alpha-amylase inhibitor, observed in all genotypes, is involved with the longer time needed for radicle protrusion, according to the band intensity difference in genotypes 07, 44 and Iapar 81.

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Bark storage Protein in Peach, Plum, and Cherry Trees

HortScience ◽

10.21273/hortsci.30.4.756a ◽

1995 ◽

Vol 30 (4) ◽

pp. 756A-756

Author(s):

M.P. Bañados ◽

M.S. Santiago ◽

C. Eterovic

Keyword(s):

Amino Acids ◽

Storage Proteins ◽

Protein Pattern ◽

Fruit Trees ◽

Sds Page ◽

Bark Storage Proteins ◽

Specific Proteins ◽

Main Protein ◽

Bark Storage Protein ◽

Cherry Trees

The main form of nitrogen reserves during overwintering are amino acids and proteins. Specific proteins called bark storage proteins (BSP) have been characterized in many tree species. To identify BSPs in `O'Henry' peach, `Angeleno' plum, and `Early Burlat' cherry trees, samples of bark were collected from January through December 1993 from trees growing under field conditions in Santiago, Chile. SDS-PAGE analyses were used to characterize the seasonal variation on the protein pattern on the bark of those Prunus species. A 60 kDa BSP was identified in the bark of all three species, which corresponds to the main protein present in the bark during the winter. This protein may play an important role as a nitrogen reserve in these fruit trees.

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Evaluation of intra-cultivar variability in Olea europaea L. cv. Leccino using morphological, biochemical and molecular markers

Australian Journal of Crop Science ◽

10.21475/ajcs.20.14.04.p2014 ◽

2020 ◽

pp. 588-596

Author(s):

Raffaella Petruccelli ◽

Deborah Beghè ◽

Tommaso Ganino ◽

Giorgio Bartolini ◽

Leonardo Ciaccheri ◽

...

Keyword(s):

Molecular Markers ◽

Olea Europaea ◽

Storage Proteins ◽

Seed Proteins ◽

Leaf Width ◽

Width Ratio ◽

Fresh Weight ◽

Fruit Length ◽

Sds Page ◽

Olea Europaéa

The phenotypic and genotypic variability of olive tree cv. Leccino (Olea europaea L.), an ancient cultivar from North-Central Italy, was investigated using 44 quantitative and qualitative agro-morphological traits, SDS-PAGE of seed proteins (storage proteins and tegument proteins) and molecular markers such as RAPDs (30 primers) and SSRs (8 primers). Fifteen accessions of Olea europaea catalogued as "Leccino" and one certified tree of "Leccino" (LESt) were examined. The plants were clonally propagated and the measuring of all morphological characteristics was conducted over a period of seven years. The ANOVA analysis showed that all accessions were homogenous for many traits while very few variations were recorded for length of one year old shoots, leaf width, leaf length/leaf width ratio, fruit length, fruit fresh weight, fruit length/fruit width ratio, pit length and pit fresh weight. The PCA analysis and similarity coefficients confirmed a low level of variability of Leccino cultivar. SDS-PAGE analysis of seed proteins showed monomorphic patterns of storage proteins. Protein subunits of teguments revealed a generally high level of similarity as evidenced by Nei-Li coefficient. SSRs and RAPDs markers showed molecular monomorphism among Leccino accessions. The results of agro-morphological, biochemical and molecular nature, taken as a whole, seem to indicate a weakly differentiated/homogeneity of the accessions tested belonging to the Leccino cultivar. The limited morphological and genetic variation could support the assumptions of a monophyletic origin of Leccino cultivar with a genetically restricted base.

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SDS–PAGE of seed proteins in Festuca (Poaceae): taxonomic implications

Canadian Journal of Botany ◽

10.1139/b91-185 ◽

1991 ◽

Vol 69 (7) ◽

pp. 1425-1432 ◽

Cited By ~ 11

Author(s):

S. G. Aiken ◽

S. E. Gardiner

Keyword(s):

Native Species ◽

Storage Proteins ◽

Polyacrylamide Gel Electrophoresis ◽

Seed Proteins ◽

Seed Storage ◽

Seed Storage Proteins ◽

Banding Patterns ◽

Ungerminated Seed ◽

Sds Page ◽

Species Specific

Taxonomically useful descriptors were provided by the banding patterns of seed storage proteins obtained when extracts of bulked, ungerminated seed samples from commercially available North American native species of Festuca were analyzed by sodium dodecylsulphate polyacrylamide gel electrophoresis (SDS–PAGE). The banding patterns for three species of rough fescues (section Breviaristatae Krivot) indicate that although the taxa are closely related, F. campestris Rydb. (2n = 56) does not appear to be an autoploid of either F. altaica Trin. (2n = 28) or F. hallii (Vasey) Piper (2n = 28). A distinct band corresponding to a molecular weight of 57 000 occurred in the seed protein profiles of all native and commercial samples of Festuca L. analyzed. The profile for F. californica Vasey, questionably section Breviaristatae, also has a band at this position, and is very different from that of F. altaica, F. campestris, and F. hallii. Species-specific banding patterns were observed for F. brachyphylla Schultes, F. saximontana Rydb., F. idahoensis Elmer, and F. trachyphylla (Hackel) Krajina (F. ovina L. s.l., F. longifolia Thuill., F. ovina var. duriuscula auct. amer.). The results support the recognition of subgenus Schedonorus (Beauv.) Peter., and sections Breviaristatae Krivot and Festuca. Key words: Poaceae, Festuca, SDS–PAGE seed proteins.

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Identification of timothy cultivars by SDS-PAGE analysis of seed storage proteins

Canadian Journal of Plant Science ◽

10.4141/cjps92-148 ◽

1992 ◽

Vol 72 (4) ◽

pp. 1215-1222 ◽

Cited By ~ 1

Author(s):

Q. Cai ◽

M. R. Bullen

Keyword(s):

Storage Proteins ◽

Seed Proteins ◽

Seed Storage ◽

Seed Storage Proteins ◽

Phleum Pratense ◽

Environmental Stability ◽

Blue Staining ◽

Coomassie Blue Staining ◽

Coomassie Blue ◽

Sds Page

SDS-PAGE analysis of seed proteins was carried out to identify the cultivars in the forage crop, timothy (Phleum pratense L.). Nineteen cultivars of timothy were examined. Among them five were from Europe and fourteen from North America. In total fifty protein bands were detected in mature seed extract by SDS-PAGE followed by Coomassie blue staining. Except for two pairs, all the cultivars were differentiated by SDS-PAGE analysis of seed storage proteins. In the electrophoretic profile, no protein bands were found to be specific either to European or to North American cultivars which is an indication of their genetic similarity. Twelve samples of cultivar Toro harvested from Alberta and Manitoba (Canada), Idaho and Minnesota (USA) were compared and no significant differences were found in their seed protein banding patterns, which suggests environmental stability of timothy seed proteins.Key words: SDS PAGE, timothy cultivar identification, seed storage proteins

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Seed storage proteins in coffee

Revista Brasileira de Fisiologia Vegetal ◽

10.1590/s0103-31312001000100004 ◽

2001 ◽

Vol 13 (1) ◽

pp. 33-40 ◽

Cited By ~ 4

Author(s):

SANDRA M. T. BAÚ ◽

PAULO MAZZAFERA ◽

LUIZ G. SANTORO

Keyword(s):

Molecular Weight ◽

Storage Proteins ◽

Protein A ◽

Gel Filtration ◽

Seed Proteins ◽

Seed Storage ◽

Seed Storage Proteins ◽

Sds Page ◽

Reserve Protein ◽

Coffee Species

It has been reported that Coffea arabica seeds contain as the main reserve protein, a legumin-like protein, constituted of two subunits, alpha and beta, of approximately 35 and 20 kDa. In this work the seed proteins of several coffee species and varieties were investigated by SDS-PAGE and gel filtration. No differences were observed in the electrophoretic profiles among varieties of C. arabica, however, marked differences were observed among species, or even among individuals of some species. In general, the molecular weight of the subunits alpha and beta accounted for a monomer of 48 to 62 kDa. However, native molecular weight obtained by gel filtration showed that for most of the species there is association of 6 of such proteins, in a hexamer. The most marked difference was observed for C. canephora and C. racemosa. The former clearly showing isoforms of the subunits, and the later showing absence of the beta subunit. The influence of proteases in this observations is discussed.

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Genetic Diversity of Common Bean Genotypes as Revealed By Seed Storage Proteins and Some Agronomic Traits

Plant Breeding and Seed Science ◽

10.2478/v10129-011-0075-1 ◽

2014 ◽

Vol 67 (1) ◽

pp. 125-137 ◽

Cited By ~ 1

Author(s):

Akbar Marzooghian ◽

Mohammad Moghaddam ◽

Mostafa Valizadeh ◽

Mohammad Hasan Kooshki

Keyword(s):

Genetic Diversity ◽

Common Bean ◽

Yield Components ◽

Storage Proteins ◽

Agronomic Traits ◽

Morphological Characteristics ◽

Seed Proteins ◽

Seed Storage ◽

Seed Storage Proteins ◽

Seed Morphology

AbstractEvaluation of the genetic diversity present within species is essential for conservation, management and utilization of the genetic resources. The objective of this study was to evaluate genetic variability of 70 common bean genotypes for seed storage proteins, grain morphological characteristics and agronomic traits. Two methods of extracting soluble seed proteins in salt were used.Positive correlations were observed among both seed morphological characters and developmental characters while yield components showed negative correlations with each other. Factor analysis for agronomic and grain morphological traits resulted in three factors were named yield components, seed morphology and phenology, respectively. Most genotypes had lower or medium scores for yield components and phenology factors. Considerable diversity was observed for seed morphology factor among the common bean genotypes.Nei’s diversity coefficient (He= 0.4), effective number of alleles (Ae= 1.69) and number of polymorphic loci (N = 17) indicated larger variation in the extraction method of soluble proteins in low salt (0.2 M NaCl) than high salt (1 M NaCl) condition. Considering that the centers of diversity for common bean are different in seed size, the result of Gst statistics showed that bands with relative mobility of 30, 32, 38 and 40 differentiated two weight groups more than other bands. Furthermore, significant differences were observed between these bands for number of pods per plant and number of seeds per plant.

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