scholarly journals Exhaled Endogenous Particles Contain Lung Proteins

2012 ◽  
Vol 58 (2) ◽  
pp. 431-440 ◽  
Author(s):  
Anna Bredberg ◽  
Johan Gobom ◽  
Ann-Charlotte Almstrand ◽  
Per Larsson ◽  
Kaj Blennow ◽  
...  
Keyword(s):  
Protein Composition ◽  
Sampling Technique ◽  
Sampling Device ◽  
Proteomic Data ◽  
Sds Page ◽  
Exhaled Air ◽  
Protein Contamination ◽  
Mascot Search Engine ◽  
High Degree ◽  
Pooled Samples

Abstract BACKGROUND We recently developed a novel, noninvasive method for sampling nonvolatile material from the distal airways. The method is based on the collection of endogenous particles in exhaled air (PEx). The aim of this study was to characterize the protein composition of PEx and to verify that the origin of PEx is respiratory tract lining fluid (RTLF). METHOD Healthy individuals exhaled into the sampling device, which collected PEx onto a silicon plate inside a 3-stage impactor. After their extraction from the plates, PEx proteins were separated by SDS-PAGE and then analyzed by LC-MS. Proteins were identified by searching the International Protein Index human database with the Mascot search engine. RESULTS Analysis of the pooled samples identified 124 proteins. A comparison of the identified PEx proteins with published bronchoalveolar lavage (BAL) proteomic data showed a high degree of overlap, with 103 (83%) of the PEx proteins having previously been detected in BAL. The relative abundances of the proteins were estimated according to the Mascot exponentially modified protein abundance index protocol and were in agreement with the expected protein composition of RTLF. No amylase was detected, indicating the absence of saliva protein contamination with our sampling technique. CONCLUSIONS Our data strongly support that PEx originate from RTLF and reflect the composition of undiluted RTLF.

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.

scholarly journals TMT-based Proteomic Analysis and Protein Expression During Excystation of Cryptosporidium Anderson

2021 ◽  
Author(s):  
Dongfang Li ◽  
Zhaohui Cui ◽  
Luyang Wang ◽  
Kaihui Zhang ◽  
Letian Cao ◽  
...  
Keyword(s):  
Proteomic Analysis ◽  
Vaccine Development ◽  
Protein Composition ◽  
Tandem Mass ◽  
Liquid Chromatograph ◽  
Control Of Gene Expression ◽  
Proteomic Data ◽  
Cryptosporidium Andersoni ◽  
New Information ◽  
Infected Adult

Abstract Background: Cryptosporidium andersoni (C. andersoni) initiates infection by the release of sporozoites through excystation. However, the proteins involved in excystation remain unknown. Researching the proteins that participate in the excystation of C. andersoni oocysts will fill the gap in our understanding of the excystation system of this parasitic pathogen. Methods: In this study, C. andersoni oocysts were collected and purified from the feces of naturally infected adult cows. Tandem mass tags (TMT) coupled with liquid chromatograph- tandem mass spectrometry (LC-MS/MS) proteomic analysis was used to investigate the proteomic expression profile of C. andersoni oocysts during excystation. Results: Our proteomic analysis identified a total of 1586 proteins, of which 17 were identified as differentially expressed proteins (DEPs), with 10 upregulated and 7 downregulated proteins. Each of those 17 proteins had multiple biological functions associated with control of gene expression at the level of transcription and biosynthetic and metabolic processes. Quantitative real-time PCR of eight selected genes validated the proteomic data.Conclusions: Our findings provide new information on the protein composition of C. andersoni oocysts as well as possible excystation factors. These data may help us to better understand the pathology of C. andersoni and thus may be useful in diagnosis, vaccine development, and immunotherapy for Cryptosporidium.

scholarly journals A species-specific nucleosomal signature defines a periodic distribution of amino acids in proteins

Open Biology ◽  
2015 ◽  
Vol 5 (4) ◽  
pp. 140218 ◽  
Author(s):  
Luis Quintales ◽  
Ignacio Soriano ◽  
Enrique Vázquez ◽  
Mónica Segurado ◽  
Francisco Antequera
Keyword(s):  
Amino Acids ◽  
Protein Composition ◽  
Open Reading Frames ◽  
Yeast Genome ◽  
Relative Distribution ◽  
Periodic Distribution ◽  
Wide Range ◽  
Average Distribution ◽  
Species Specific ◽  
High Degree

Nucleosomes are the basic structural units of chromatin. Most of the yeast genome is organized in a pattern of positioned nucleosomes that is stably maintained under a wide range of physiological conditions. In this work, we have searched for sequence determinants associated with positioned nucleosomes in four species of fission and budding yeasts. We show that mononucleosomal DNA follows a highly structured base composition pattern, which differs among species despite the high degree of histone conservation. These nucleosomal signatures are present in transcribed and non-transcribed regions across the genome. In the case of open reading frames, they correctly predict the relative distribution of codons on mononucleosomal DNA, and they also determine a periodicity in the average distribution of amino acids along the proteins. These results establish a direct and species-specific connection between the position of each codon around the histone octamer and protein composition.

scholarly journals STUDY OF ANTIMICROBIAL PROTEIN FROM THE HEMOLYMPH OF FRESHWATER CRAB OZIOTELPHUSA SENEX SENEX AND ITS EFFICACY AGAINST THE HUMAN PATHOGENS

2018 ◽  
Vol 11 (4) ◽  
pp. 427
Author(s):  
Sumalatha D ◽  
Nithya Tg ◽  
Jayanthi J ◽  
Ragunathan Mg
Keyword(s):  
Antimicrobial Activity ◽  
Molecular Mass ◽  
Search Engine ◽  
Maldi Ms ◽  
Antimicrobial Protein ◽  
Freshwater Crab ◽  
Gram Positive ◽  
Gram Negative ◽  
Sds Page ◽  
Mascot Search Engine

 Objective: The study was done to isolate the antimicrobial protein from the freshwater crab.Methods: Antimicrobial protein was purified by sequential step of ammonium sulfate precipitation, dialysis, ion exchange chromatography, and fast protein liquid chromatography. The apparent molecular mass was determined by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) and matrix-assisted laser desorption ionization-mass spectrometry (MALDI-MS/MS). Primary structure analysis was done from MASCOT search engine. The antimicrobial activity of the protein was done using well diffusion method against Gram-positive and Gram-negative bacteria.Results: The molecular mass of antimicrobial protein was determined to be 33KDa by SDS-PAGE and MALDI-MS/MS. The antimicrobial protein contains eight peptides which were determined by MASCOT search engine. The protein exhibited antimicrobial activity both for Gram-positive and Gram-negative bacteria.Conclusion: The results could provide information for investigating the antimicrobial protein derived from the hemolymph of the freshwater crab Oziotelphusa senex senex.

CO2-controlled sampling of alveolar gas in mechanically ventilated patients

2001 ◽  
Vol 90 (2) ◽  
pp. 486-492 ◽  
Author(s):  
Jochen K. Schubert ◽  
Karl-Heinz Spittler ◽  
Guenther Braun ◽  
Klaus Geiger ◽  
Josef Guttmann
Keyword(s):  
Dead Space ◽  
Coefficient Of Variation ◽  
Sampling Technique ◽  
Sampling Device ◽  
Mechanically Ventilated ◽  
Mechanically Ventilated Patients ◽  
Selective Enrichment ◽  
Gas Sampling ◽  
End Tidal ◽  
Ventilated Patients

A newly designed gas-sampling device using end-tidal CO2to separate dead space gas from alveolar gas was evaluated in 12 mechanically ventilated patients. For that purpose, CO2-controlled sampling was compared with mixed expiratory sampling. Alveolar sampling valves were easily controlled via CO2concentration. Concentrations of four volatile substances were determined in the expired and inspired gas. Isoflurane and isoprene, which did not occur in the inspired air, had ratios of end-tidal to mixed expired concentrations of 1.75 and 1.81, respectively. Acetone and pentane, found in both the inspired and expired air, showed ratios of 0.96 and 1.0, respectively. Precision of concentration measurements was between 2.4% (isoprene) and 11.2% (isoflurane); reproducibility (as coefficient of variation) was 5%. Because the only possible source of isoflurane and isoprene in this setting was patients' blood, selective enrichment of alveolar gas was demonstrated. By using the new sampling technique, sensitivity of breath analysis was nearly doubled.

scholarly journals Analysis of a rare recombination event within the multigenic Hor 2 locus of barley (Hordeum vulgare L.)

1990 ◽  
Vol 55 (3) ◽  
pp. 171-176 ◽  
Author(s):  
Peter R. Shewry ◽  
Saroj Parmar ◽  
Julian Franklin ◽  
Shirley R. Burgess
Keyword(s):  
Hordeum Vulgare ◽  
Recombination Event ◽  
Rflp Analysis ◽  
Genomic Clone ◽  
Class I ◽  
Class Iii ◽  
Hordeum Vulgare L ◽  
Ancestral Gene ◽  
Sds Page ◽  
High Degree

SummaryA rare recombinant within the multigenic Hor 2 locus of barley was detected by SD-PAGE of hordein fractions from F2 grain from the cross Bomi × P12/3. Analysis of a homozygous F4 line by 2-D IEF/SDS-PAGE showed that recombination between the class I/II and class III subfamilies of genes had occurred, indicating that they are spatially separate within the Hor 2 locus. RFLP analysis using a B hordein-related cDNA clone confirmed that recombination had occurred, while similar analysis using a genomic clone related to γ-type hordein (encoded by the Hor 5/HrdF locus) indicated the order of the two subfamilies of genes on the short arm of chromosome 5, the class I/II genes being closer to the centromere. The results are consistent with the origin of the B hordein gene family from initial duplication of a single ancestral gene to give two genes which diverged to become the ancestors of the class I/II and class III subfamilies. Subsequent cycles of duplication and divergence have resulted in the present high degree of polymorphism.

Changes in total and individual proteins during drying and ruminal fermentation of alfalfa

2005 ◽  
Vol 2005 ◽  
pp. 198-198
Author(s):  
A. A. Sadeghi ◽  
P. Shawrang ◽  
M. Moradi ◽  
A. Nikkhah
Keyword(s):  
Crude Protein ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Protein Composition ◽  
Plant Proteins ◽  
Ruminal Fermentation ◽  
Protein Nitrogen ◽  
Sds Page ◽  
Total Crude Protein ◽  
Hydrolysis Of

Proteolysis within plant cells occurs during wilting and drying. Changes in plant proteins during those periods usually are monitored by measurement of total crude protein and non protein nitrogen. Alternatively, changes in concentrations of individual proteins can be measured. Plants are composed of an array of different proteins. Electrophoresis can be used to separate these proteins and has been used to study effects of wilting and ensiling on proteins of some forages (Grum et al., 1991). Electrophoresis also has been used in the study of ruminal hydrolysis of oilseed meals proteins (Sadeghi et al., 2004). Most of the experiments designed to use electrophoresis to study protein metabolism in forages and ruminants have been qualitative. The main objective of this study was to determine whether sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE) and densitometry could be used to monitor quantitatively the changes in alfalfa protein composition during wilting, drying and ruminal exposure.

scholarly journals Self-concept and Family: A study on Greek secondary school students

2016 ◽  
Vol 10 (1) ◽  
Author(s):  
Dimitris Kiritsis
Keyword(s):  
Sampling Technique ◽  
Self Concept ◽  
School Students ◽  
The Family ◽  
Major Variation ◽  
Essential Contribution ◽  
The One ◽  
High Degree ◽  
The Relationship

The aim of the study is twofold. On the one hand it concerns the measurement and the examination of the subjects’ self-concept and on the other the detection and justification of the role of family in its configuration. The study analyzed the data collected from the answers to a research questionnaire of 1344 15-and 16-year-old school students in the Prefecture of Thessaloniki, Greece) with the use of a stratified random sampling technique. The first important finding concerned the high degree of the general self-concept of the adolescents. Among the seven specific sectors of the general self-concept a major variation was noted, with the higher average to be traced in the relationship that the students have configured with their peers and the lower one in the valuation of their academic competence. The second important finding was the ascertainment of the essential contribution of the family.

scholarly journals Characterization and purification of a novel dATP-binding protein in eukaryotes

1992 ◽  
Vol 287 (3) ◽  
pp. 871-879 ◽  
Author(s):  
A Dalton ◽  
D P Hornby ◽  
S P Langston ◽  
G M Blackburn
Keyword(s):  
Binding Protein ◽  
Active Form ◽  
Direct Interaction ◽  
Nuclear Fraction ◽  
Yeast Saccharomyces Cerevisiae ◽  
Naturally Occurring ◽  
Sds Page ◽  
Marked Preference ◽  
High Degree ◽  
Page Electrophoresis

We characterized and purified an acidic dATP-binding protein, which, in its active form, resides in the nuclear fraction of a range of cells from mammals (including pig liver) and baker's yeast (Saccharomyces cerevisiae). This protein exhibits a high degree of specificity for the deoxy form of the naturally occurring nucleoside triphosphates and shows a marked preference for the purine deoxynucleoside triphosphates dATP and dGTP. The protein cleaves the terminal phosphate of dATP and appears to retain the dADP moiety of the nucleotide in a reaction that is resistant to both SDS and 8 M-urea. Fractionation of the nuclear preparation followed by non-denaturing PAGE and SDS/PAGE electrophoresis was sufficient to produce pure protein. The occurrence of this activity in all nuclei tested suggests that it plays an important role in nuclear metabolism. The specificity of the enzyme for deoxynucleoside triphosphates further suggests a role for this enzyme in DNA replication or repair, but the acidity of the protein argues against a direct interaction with DNA, and, indeed, the catalytic activity is not modulated by the inclusion of DNA in a variety of physical forms.

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