scholarly journals Vicilin and legumin storage proteins are abundant in water and alkali soluble protein fractions of glandless cottonseed

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Zhongqi He ◽  
Christopher P. Mattison ◽  
Dunhua Zhang ◽  
Casey C. Grimm
Keyword(s):  
Mass Spectrometry ◽  
Soluble Protein ◽  
Extraction Efficiency ◽  
Storage Proteins ◽  
Protein Composition ◽  
Protein Fractions ◽  
Peptide Fragments ◽  
2S Albumin ◽  
Cottonseed Protein ◽  
Glandless Cottonseed

AbstractIn this work, we sequentially extracted water (CSPw)- and alkali (CSPa)-soluble protein fractions from glandless cottonseed. SDS-Gel electrophoresis separated CSPw and CSPa to 8 and 14 dominant polypeptide bands (110–10 kDa), respectively. Liquid chromatography-electrospray ionization-tandem mass spectrometry identified peptide fragments from 336 proteins. While the majority of peptides were identified as belonging to vicilin and legumin storage proteins, peptides from other functional and uncharacterized proteins were also detected. Based on the types (unique peptide count) and relative abundance (normalized total ion current) of the polypeptides detected by mass spectrometry, we found lower levels (abundance) and types of legumin isoforms, but higher levels and more fragments of vicilin-like antimicrobial peptides in glandless samples, compared to glanded samples. Differences in peptide fragment patterns of 2S albumin and oleosin were also observed between glandless and glanded protein samples. These differences might be due to the higher extraction recovery of proteins from glandless cottonseed as proteins from glanded cottonseed tend to be associated with gossypol, reducing extraction efficiency. This work enriches the fundamental knowledge of glandless cottonseed protein composition. For practical considerations, this peptide information will be helpful to allow better understanding of the functional and physicochemical properties of glandless cottonseed protein, and improving the potential for food or feed applications.

scholarly journals Seed Storage Proteins, 2S Albumin And 11S Globulin, Associated to Severe Allergic Reactions after Flaxseed Intake

2021 ◽  
Vol 32 (5) ◽  
Author(s):  
C Bueno-Díaz ◽  
C Biserni ◽  
L Martín-Pedraza ◽  
M de las Heras ◽  
C Blanco ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Storage Proteins ◽  
Binding Capacity ◽  
Seed Storage ◽  
Seed Storage Proteins ◽  
Cross Reactivity ◽  
2S Albumin ◽  
11S Globulin ◽  
Flaxseed Extract

Background: Given the increased popularity of flaxseed in meals, several cases of allergy to these seeds have been reported. Little is known about allergens implicated in hypersensitivity reactions to these seeds. The present work aimed to identify the allergens involved in IgE-mediated reactions in five patients with a clinical history of severe systemic symptoms after flaxseed consumption. Methods: Proteins susceptible to be allergens with IgE-binding capacity were purified from flaxseed extract by chromatographic techniques. Their identification was achieved via MALDI-TOF mass spectrometry. Immunoassays were performed using the five allergic patient’s era either by testing them individually or as a pool. Results: Four out of five patients recognized a low-molecular-mass protein (around 13kDa) by immunoblotting of the flaxseed extract, while two patients recognized a protein of approximately 55 kDa. They were identified by mass spectrometry as flaxseed 2S albumin, included into WHO/IUIS allergen nomenclature as Lin u 1,and 11S globulin, respectively. Inhibition assays revealed in vitro IgE-cross-reactivity of Lin u 1 with peanut and cashew nut proteins, while IgE recognition of 11S globulin by patients’ sera was partially inhibited by several plant-derived sources. Conclusions: Seed storage proteins from flaxseed were involved in the development of severe symptoms in five individuals and exhibited cross-reactivity with other allergenic sources. Besides the severity of flaxseed allergy in patients sensitized to 2S albumin, it is the first time that the 11S globulin is identified as a potential allergen. We consider that these data should be taken into account for a more accurate diagnosis of patients.

scholarly journals Influence of Organic and Conventional Farming on Grain Yield and Protein Composition of Chickpea Genotypes

Agronomy ◽  
2021 ◽  
Vol 11 (2) ◽  
pp. 191
Author(s):  
Michele Andrea De Santis ◽  
Michele Rinaldi ◽  
Valeria Menga ◽  
Pasquale Codianni ◽  
Luigia Giuzio ◽  
...  
Keyword(s):  
Grain Yield ◽  
Organic Farming ◽  
Cropping Systems ◽  
Negative Relationship ◽  
Cropping System ◽  
Protein Composition ◽  
2S Albumin ◽  
Sds Page ◽  
Health Quality ◽  
Water Holding

Chickpea is a key crop in sustainable cropping systems and for its nutritional value. Studies on agronomic and genetic influences on chickpea protein composition are missing. In order to obtain a deep insight into the genetic response of chickpeas to management in relation to agronomic and quality traits, a two-year field trial was carried out with eight chickpea genotypes under an organic and conventional cropping system. Protein composition was assessed by SDS-PAGE in relation to the main fractions (vicilin, convicilin, legumin, lectin, 2s-albumin). Crop response was highly influenced by year and presumably also by management, with a −50% decrease in grain yield under organic farming, mainly due to a reduction in seed number per m2. No effect of crop management was observed on protein content, despite significant differences in terms of protein composition. The ratio between the major globulins, 7s vicilin and 11s legumin, showed a negative relationship with grain yield and was found to be higher under organic farming. Among genotypes, black-seed Nero Senise was characterized by the highest productivity and water-holding capacity, associated with low lectin content. These findings highlight the importance of the choice of chickpea genotypes for cultivation under organic farming in relation to both agronomic performance and technological and health quality.

scholarly journals Comparative Analysis of Electrophoretic Profile of Major Proteins of Milk from Alpine and Carpathian Goats

2017 ◽  
Vol 74 (1) ◽  
pp. 20 ◽  
Author(s):  
Alina NASALEAN ◽  
Laurentiu OGNEAN ◽  
Sergiu MUNTEAN ◽  
Stefana BALICI ◽  
Horea MATEI
Keyword(s):  
Protein Profile ◽  
Milk Proteins ◽  
Goat Milk ◽  
Protein Composition ◽  
Raw Milk ◽  
Biologically Active ◽  
Protein Fractions ◽  
Animal Nutrition ◽  
Sds Page ◽  
Percentage Data

The milk’s proteins provide nutritional and biologically active values, essential in human and animal nutrition. In the case of goat milk, the proteins’ concentration and quality represent basic indices for the evaluation of the nutritional and biologically active values. The proposal is to comparatively analyse the protein profile of milk. The milk was collected from two different breeds: French Alpine and Romanian Carpathian. During March and April 2016 there were collected samples of raw milk in hygienic and sanitation conditions. There were two lots: first lot has 10 Carpathian goats and the second lot has 10 Alpine goats. The protein composition of goat milk was established with SDS-PAGE, after the evaluation of the total proteins’ concentration with the Bradford method. The quantitative and percentage data obtained with electrophoresis revealed few differences between those 8 identified protein fractions. Between those two lots, regarding the levels of β-CN, k-CN and β-lactoglobulines there were significant differences. The other protein fractions have values almost identical. Statistical analysis of obtained data shaped the differences in the protein profile at those two breeds. Based on those differences it is to note the superior potential of the Alpine breed regarding the content in biologically active milk proteins. Regarding the obtained data, this study brings new contributions for the evaluation and analysis of protein profile as a nutritive and biologically active component of goat milk, confirming its character as a functional aliment.

Large-scale N-glycoproteome map of rat brain tissue: Simultaneous characterization of insoluble and soluble protein fractions

PROTEOMICS ◽  
2011 ◽  
Vol 11 (21) ◽  
pp. 4274-4278 ◽  
Author(s):  
Xiaoqiang Qiao ◽  
Dingyin Tao ◽  
Yanyan Qu ◽  
Liangliang Sun ◽  
Liang Gao ◽  
...  
Keyword(s):  
Rat Brain ◽  
Brain Tissue ◽  
Soluble Protein ◽  
Large Scale ◽  
Protein Fractions ◽  
Rat Brain Tissue

The high-resolution mass spectrometry study of the protein composition of amyloid-like urine aggregates associated with preeclampsia

2019 ◽  
Vol 26 (2) ◽  
pp. 158-161 ◽  
Author(s):  
Victoria A Sergeeva ◽  
Natalia V Zakharova ◽  
Anna E Bugrova ◽  
Natalia L Starodubtseva ◽  
Maria I Indeykina ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
High Resolution ◽  
Pregnant Women ◽  
Congo Red ◽  
Molecular Mechanisms ◽  
High Resolution Mass Spectrometry ◽  
Protein Composition ◽  
High Resolution Mass ◽  
Proteomic Approach ◽  
Resolution Mass

The study of protein misfolding and post-translational processing abnormalities is a promising diagnostic approach for socially significant pathologies associated with the accumulation of abnormal forms of proteins. Recently, it was shown that amyloid-like aggregates can be observed in the urine of pregnant women with preeclampsia, which is the most severe hypertensive complication that can lead to fateful outcomes. The protein composition of urine aggregates may clarify the molecular mechanisms underlying the pathology and has not yet been studied in detail. Using a proteomic approach based on high-resolution mass spectrometry, we studied the protein composition of amyloid-like structures that aggregate in the presence of Congo red azo-dye in the urine of pregnant women with preeclampsia. Fragments of β-sheets of α-1-antitrypsin, complement 3, haptoglobin, ceruloplasmin, and trypstatin were identified as most likely targets for Congo red binding.

scholarly journals Variation of Detailed Protein Composition of Cow Milk Predicted from a Large Database of Mid-Infrared Spectra

Animals ◽  
2019 ◽  
Vol 9 (4) ◽  
pp. 176 ◽  
Author(s):  
Marco Franzoi ◽  
Giovanni Niero ◽  
Giulio Visentin ◽  
Mauro Penasa ◽  
Martino Cassandro ◽  
...  
Keyword(s):  
Infrared Spectra ◽  
Protein Composition ◽  
Protein Fractions ◽  
Cow Milk ◽  
Fat Percentage ◽  
Dual Purpose ◽  
Factors Affecting ◽  
Dual Purpose Cattle ◽  
Milk Urea ◽  
Β Lactoglobulin

This study aimed to investigate factors affecting protein fractions, namely α-casein (α-CN), β-casein (β-CN), κ-casein (κ-CN), β-lactoglobulin (β-LG) and α-lactalbumin (α-LA) predicted from milk infrared spectra in milk of dairy and dual-purpose cattle breeds. The dataset comprised 735,328 observations from 49,049 cows in 1782 herds. Results highlighted significant differences of protein fractions in milk of the studied breeds. Significant variations of protein fractions were found also through parities and lactation, with the latter thoroughly influencing protein fractions percentage. Interesting correlations (r) were estimated between β-CN, κ-CN and β-LG, expressed as percentage of crude protein, and milk urea nitrogen (r = 0.31, −0.20 and −0.26, respectively) and between α-LA and fat percentage (r = 0.41). The present study paves the way for future studies on the associations between protein fractions and milk technological properties, and for the estimation of genetic parameters of predicted protein composition.

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