scholarly journals Differentially expressed plasma protein fractions in workers of dyeing unit at a textile industry and comparable controls

2015 ◽  
Vol 49 (2) ◽  
pp. 89-94
Author(s):  
N Roohi ◽  
A Shaukat ◽  
MA Iqbal ◽  
T Mumtaz
Keyword(s):  
Health Status ◽  
Adverse Effects ◽  
Plasma Protein ◽  
Textile Industry ◽  
Plasma Proteins ◽  
T Test ◽  
Protein Fractions ◽  
Significant Decrement ◽  
Textile Dyeing ◽  
Sds Page

Workers of textile industry are exposed to different hazardous chemicals that cause adverse effects on their health. As variations in plasma proteins are the best indicators of health status of the subjects, hence, we compared plasma protein fractions, resolved by SDS-PAGE of textile dyeing industry workers (n=30) with control subjects (n=30). Proteins were quantified by Total Lab Quant software and analyzed, statistically, by Student t-test. Thirteen protein fractions were detected ranging 250-17kDa. A significant increase in 132 and 53kDa fractions, whereas, a significant decrement in 87 and 66kDa fractions with a highly significant reduction in 112kDa fraction was observed. However, 250, 224, 43, 23, 19 and 17kDa protein fractions did not vary considerably. As some proteins circulate only during particular physiological or pathological circumstances and may serve as biomarkers of anomalies, the altered expressions of these biomolecules observed in textile dyeing industry workers may be strong predictors of different ailments. DOI: http://dx.doi.org/10.3329/bjsir.v49i2.22002 Bangladesh J. Sci. Ind. Res. 49(2), 89-94, 2014

scholarly journals Plasma proteins of young African catfish (Clarias gariepinus, Burchell 1822).

1987 ◽  
Vol 35 (4) ◽  
pp. 521-524
Author(s):  
J.H. Boon ◽  
J.M. Smits ◽  
T. Wensing ◽  
E. Lo
Keyword(s):  
Health Status ◽  
Water Supply ◽  
Plasma Protein ◽  
Negative Correlation ◽  
Plasma Proteins ◽  
Clarias Gariepinus ◽  
Total Content ◽  
African Catfish ◽  
Feeding Level ◽  
Effect Of Feeding

The effect of feeding level and water supply on the total content of plasma protein (TPP) and fractions of these proteins (PPF) of young African catfish was studied. It was found that TPP can be divided into 4 fractions (PPF I-IV), of which PPF I is predominant. Analysis of the results showed a strong effect of feeding level on TPP and PPF I-IV. There was a positive correlation between TPP and the weights of PPF I-IV, and a negative correlation between PPF I and PPF II. The PPF I fraction might be usable as an indicator for the health status of young catfishes. (Abstract retrieved from CAB Abstracts by CABI’s permission)

scholarly journals PROTEOLYTIC ENZYMES

1949 ◽  
Vol 33 (2) ◽  
pp. 103-124 ◽  
Author(s):  
David Grob
Keyword(s):  
Plasma Protein ◽  
Inhibitory Activity ◽  
Plasma Proteins ◽  
Proteolytic Enzymes ◽  
Lima Bean ◽  
Egg White ◽  
Protein Fractions ◽  
High Concentration ◽  
Heat Stable ◽  
Very High

1. Serum proteinase precursor was found in plasma protein fractions I and III of Cohn. Inhibitors of serum proteinase, leucoproteinase, trypsin, and papain were found in fractions IV-1 and IV-4, and to a lesser extent in fractions V and I. 2. Pancreatic, soy bean, lima bean, and egg white inhibitors inhibited trypsin stoichiometrically. Pancreatic inhibitor had comparable inhibitory activity against serum proteinase; soy bean inhibitor had somewhat less, lima bean inhibitor even less, and egg white inhibitor very little. None of these inhibitors appreciably inhibited leucoproteinase or papain. 3. Serum and fractions IV - 1 and IV - 4 had marked inhibitory activity against trypsin and leucoproteinase, and somewhat less against serum proteinase and papain. The inhibitory activity of the plasma proteins against trypsin and leucoproteinase was due almost entirely to fractions IV - 1 and IV - 4; against serum proteinase and papain fraction V was slightly more important. The "reconstituted plasma proteins" accounted for 8 to 25 per cent of the proteinase-inhibitory activity of whole serum or plasma. 4. The proteinase-inhibitory activity of serum, plasma protein fractions, and soy bean inhibitor was heat labile, while that of pancreatic, lima bean, and egg white inhibitors was relatively heat stable. 5. Reducing and oxidizing agents, in very high concentration, inhibited serum proteinase, as well as trypsin and leucoproteinase. These proteinases were not influenced by mercurial sulfhydryl inhibitors, indicating that free sulfhydryl groups do not play an important part in their activity.

scholarly journals Integrative genetic and immune cell analysis of plasma proteins in healthy donors identifies novel associations involving primary immune deficiency genes

2021 ◽  
Author(s):  
Barthelemy Caron ◽  
Etienne Patin ◽  
Maxime Rotival ◽  
Bruno Charbit ◽  
Matthew L Albert ◽  
...  
Keyword(s):  
Health Status ◽  
Blood Cell ◽  
Plasma Protein ◽  
Plasma Proteins ◽  
Genetic Factors ◽  
Immune Cell ◽  
Individual Variability ◽  
Genetic Associations ◽  
Protein Levels ◽  
Age And Sex

Blood plasma proteins play an important role in immune defense against pathogens, including cytokine signaling, the complement system and the acute-phase response. Recent large-scale studies have reported genetic (i.e. quantitative trait loci, pQTLs) and non-genetic factors, such as age and sex, as major determinants to inter-individual variability in immune response variation. However, the contribution of blood cell composition to plasma protein heterogeneity has not been fully characterized and may act as a confounding factor in association studies. Here, we evaluated plasma protein levels from 400 unrelated healthy individuals of western European ancestry, who were stratified by sex and two decades of life (20-29 and 60-69 years), from the Milieu Interieur cohort. We quantified 297 proteins by Luminex in a clinically certified laboratory and their levels of variation were analysed together with 5.2M single-nucleotide polymorphisms. With respect to non-genetic variables, we included more than 700 lifestyle and biochemical factors, as well as counts of seven circulating immune cell populations measured by hemogram and standardized flow cytometry. Collectively, we found 152 significant associations involving 49 proteins and 20 non-genetic variables. Consistent with previous studies, age and sex showed a global, pervasive impact on plasma protein heterogeneity, while body mass index and other health status variables were among the non-genetic factors with the highest number of associations. After controlling for these covariates, we identified 100 and 12 pQTLs acting in cis and trans, respectively, collectively associated with 87 plasma proteins and including 30 novel genetic associations. Genetic factors explained the largest fraction of the variability of plasma protein levels, as compared to non-genetic factors. In addition, blood cell fractions, including leukocytes, lymphocytes and three types of polymorphonuclear cells, had a larger contribution to inter-individual variability than age and sex, and appeared as confounders of specific genetic associations. Finally, we identified new genetic associations with plasma protein levels of eight monogenic Mendelian disease genes including three primary immunodeficiency genes (Ficolin-3, Interleukine-2 Receptor alpha and FAS). Our study identified novel genetic and non-genetic factors associated to plasma protein levels which may inform health status and disease management.

Comparative evaluation of plasma protein purification and 2-D gel electrophoresis protocols for analysis of HIV-1 infected plasma proteins (Preprint)

2021 ◽  
Author(s):  
Mr Sushanta Kumar Barik Sr ◽  
Deepika Varshney ◽  
Deepa Bisht Sr ◽  
Shripad A Patil Sr ◽  
Rananjaya Singh Sr ◽  
...  
Keyword(s):  
Protein Purification ◽  
Human Plasma ◽  
Plasma Protein ◽  
Gel Electrophoresis ◽  
Comparative Evaluation ◽  
Plasma Proteins ◽  
Human Plasma Protein ◽  
Sds Page ◽  
Hiv 1 ◽  
Abundance Proteins

BACKGROUND The focus of the study was the comparative evaluation of HIV-1 infected plasma protein purification and 2-D gel electrophoresis protocols. OBJECTIVE Human plasma protein purification is a risk task to perform 2-D gel electrophoresis. Human plasma proteins contain nearly 70% albumin and globulin. The removal of such high abundance high molecular weight proteins is very difficult to perform 2-D gel electrophoresis METHODS To the best of our knowledge, we searched several research papers, developed and adopted various organic and non-organic based protocols for HIV-1 infected human plasma protein purification and various isoelectrofocusing protocols in 2-D gel electrophoresis RESULTS After failure in 2-D gel-electrophoresis performance by these protocols, Aurum serum mini kit (Bio-Rad, USA) was adopted for plasma protein purification for performing 2-D gel electrophoresis. The low-abundance proteins were better resolved by 10% SDS-PAGE in 2-D gel-electrophoresis. Then, we extended the MALDI-TOF/TOF analysis of low-abundance proteins in human plasma by adopting the Aurum serum mini kit ( Bio-Rad, USA) for 2-D gel electrophoresis. CONCLUSIONS Thus, we concluded that, the Aurum serum mini kit (Bio-Rad, USA) is best to perform the 2-D gel electrophoresis of HIV-1 infected human plasma by depleting the high abundant proteins like albumin and globulin

scholarly journals Plasma electrophoresis profiles of Blanding’s turtles (Emydoidea blandingii) and influences of month, age, sex, health status, and location

PLoS ONE ◽  
2021 ◽  
Vol 16 (10) ◽  
pp. e0258397
Author(s):  
Kirsten E. Andersson ◽  
Laura Adamovicz ◽  
Lauren E. Mumm ◽  
Samantha E. Bradley ◽  
John M. Winter ◽  
...  
Keyword(s):  
Health Status ◽  
Environmental Factors ◽  
Plasma Protein ◽  
Geographical Location ◽  
Reproductive Activity ◽  
Protein Fractions ◽  
Emydoidea Blandingii ◽  
Age Class ◽  
Lower Protein ◽  
Free Ranging

Baseline plasma electrophoresis profiles (EPH) are important components of overall health and may aid in the conservation and captive management of species. The aim of this study was to establish plasma protein fractions for free-ranging Blanding’s turtles (Emydoidea blandingii) and evaluate differences due to age class (adult vs. sub-adult vs. juvenile), sex (male, female, or unknown), year (2018 vs. 2019), month (May vs. June vs. July), health status, and geographical location (managed vs. unmanaged sites). Blood samples were obtained from 156 Blanding’s turtles in the summer of 2018 and 129 in 2019 at two adjacent sites in Illinois. Results of the multivariate analysis demonstrated that age class, sex, year, month, health status, and geographical location all contributed to the variation observed in free-ranging populations. Adult females had the highest concentration of many protein fractions, likely associated with reproductive activity. Juveniles had lower protein concentrations. Temperature and rainfall differences between years impacted concentrations between 2018 and 2019, while May and June of both years saw higher levels in some protein fractions likely due to peak breeding and nesting season. Individuals with evidence of trauma or disease also showed increased plasma protein fractions when compared to those that were considered healthy. The two sites showed a wide/large variation over the two years. All of these factors emphasize the importance of considering multiple demographic or environmental factors when interpreting the EPH fractions. Establishing ranges for these analytes will allow investigation into disease prevalence and other environmental factors impacting this endangered species.

Microvascular permeability to endogenous plasma proteins in the jejunum

1990 ◽  
Vol 258 (6) ◽  
pp. H1650-H1654
Author(s):  
N. A. Mortillaro ◽  
A. E. Taylor
Keyword(s):  
Plasma Protein ◽  
Plasma Proteins ◽  
Protein Fractions ◽  
Total Proteins ◽  
Venous Outflow ◽  
Independent State ◽  
A Value ◽  
Gradient Gel Electrophoresis ◽  
Osmotic Reflection Coefficient ◽  
Molecular Radius

Steady-state lymph flow and lymph (CL) and plasma (CP) protein concentrations were measured at venous outflow pressures of 0, 10, 20, and 30 mmHg in an autoperfused segment of cat jejunum. In addition to determining total protein concentrations in lymph and plasma, polyacrylamide gradient gel electrophoresis was used to determine lymph and plasma protein concentrations of albumin and nine other plasma proteins. The osmotic reflection coefficient (sigma d) for total proteins, albumin, and each of the nine protein fractions was estimated using CL/CP at a capillary filtration rate independent state, when 1 - CL/CP = sigma d. A sigma d of 0.83 was obtained for total proteins, a value similar to that reported for both dog jejunum and descending colon (0.85) but appreciably different from that reported for both cat stomach (0.78) and ileum (0.92). Additionally, sigma d for albumin and each of the nine plasma protein fractions (molecular radii ranging from 37 to 120 A) increased as molecular radius increased. A two-pore model composed of a ratio of 3,750 48-A radius small pores to one 250-A radius large pore describes the data obtained, with 82% of the total volume flow occurring through the small pores and 16% through the large pores.

scholarly journals Comparative evaluation of plasma protein purification and 2-D gel electrophoresis protocols for analysis of HIV-1 infected human plasma proteins

2021 ◽  
Author(s):  
Sushanta Kumar Barik ◽  
Deepika Varshney ◽  
Keshar Kunja Mohanty ◽  
Deepa Bisht ◽  
Shripad A. Patil ◽  
...  
Keyword(s):  
Protein Purification ◽  
Human Plasma ◽  
Plasma Protein ◽  
Gel Electrophoresis ◽  
Comparative Evaluation ◽  
Plasma Proteins ◽  
Sds Page ◽  
High Molecular Weight Proteins ◽  
Hiv 1 ◽  
Abundance Proteins

Abstract Purification of proteins from human plasma is a herculean task to perform 2-D gel electrophoresis. Human plasma contains nearly 70% albumin and globulin. The removal of such high abundance high molecular weight proteins is very difficult before performing 2-D gel electrophoresis. It becomes more difficult when we intent to investigate in infectious diseases like HIV/AIDS. We tried to the best of our efforts adopting various organic and non-organic based protocols based on various published papers. After failure of these protocols in results of 2-D gel-electrophoresis Aurum serum mini kit (Bio-Rad, USA) was adopted for plasma protein purification for performing 2-D gel electrophoresis. The low-abundance proteins were better resolved by 10% SDS-PAGE in 2-D gel-electrophoresis. Then,we extended the MALDI-TOF/TOF analysis of low-abundance proteins in human plasma by adopting the Aurum serum mini kit (Bio-Rad, USA) for 2-D gel electrophoresis. Thus, we concluded that, depletion of high abundant proteins like albumin and globulin, the use of the Aurum serum mini kit (Bio-Rad, USA) is the protocol of choice to perform the 2-D gel electrophoresis of HIV-1 infected human plasma.

Vasoactive properties of plasma protein fractions

1964 ◽  
Vol 206 (4) ◽  
pp. 923-925 ◽  
Author(s):  
M. Wurzel ◽  
R. C. Bacon ◽  
R. B. Kalt ◽  
B. W. Zweifach
Keyword(s):  
Plasma Protein ◽  
Plasma Proteins ◽  
Vascular Tone ◽  
Test Dose ◽  
Protein Fractions ◽  
Maximal Effect ◽  
Threshold Test ◽  
Aortic Strip ◽  
Rabbit Aortic Strip ◽  
Albumin Content

The capacity of plasma to potentiate norepinephrine (NOR)-induced contractions of the rabbit aortic strip can be attributed to the plasma protein fractions, perhaps almost exclusively to their albumin content. Albumin, 0.2–2 mg/15 ml, potentiated a threshold test dose of NOR from minimal to maximal effect. In the presence of albumin 1–2 mg/15 ml, the threshold dose of NOR was decreased about five to ten times. Albumin, 500 mg/15 ml, did not have a greater potentiating effect. Albumin itself had no contracting ability. The blood of the anesthetized rabbit does not contain sufficient NOR to contract the aortic strip; such concentrations of NOR even in the presence of plasma proteins or albumin were ineffective. The data suggest that NOR does not contribute directly to the maintenance of normal vascular tone.

scholarly journals Hypochlorite-induced oxidation of proteins in plasma: formation of chloramines and nitrogen-centred radicals and their role in protein fragmentation

1999 ◽  
Vol 340 (2) ◽  
pp. 539-548 ◽  
Author(s):  
Clare L. HAWKINS ◽  
Michael J. DAVIES
Keyword(s):  
Plasma Protein ◽  
Plasma Proteins ◽  
Dependent Manner ◽  
Concentration Dependent Manner ◽  
Nitrobenzoic Acid ◽  
Parent Protein ◽  
Sds Page ◽  
Amine Groups ◽  
Epr Spin Trapping ◽  
Protein Fragmentation

Activated phagocyte cells generate hypochlorite (HOCl) via the release of H2O2 and the enzyme myeloperoxidase. Plasma proteins are major targets for HOCl, although little information is available about the mechanism(s) of oxidation. In this study the reaction of HOCl (at least 50 μM) with diluted fresh human plasma has been shown to generate material that oxidizes 5-thio-2-nitrobenzoic acid; these oxidants are believed to be chloramines formed from the reaction of HOCl with protein amine groups. Chloramines have also been detected with isolated plasma proteins treated with HOCl. In both cases chloramine formation accounts for approx. 20-30% of the added HOCl. These chloramines decompose in a time-dependent manner when incubated at 20 or 37 °C but not at 4 °C. Ascorbate and urate remove these chloramines in a time- and concentration-dependent manner, with the former being more efficient. The reaction of fresh diluted plasma with HOCl also gives rise to protein-derived nitrogen-centred radicals in a time- and HOCl-concentration-dependent manner; these have been detected by EPR spin trapping. Identical radicals have been detected with isolated HOCl-treated plasma proteins. Radical formation was inhibited by excess methionine, implicating protein-derived chloramines (probably from lysine side chains) as the radical source. Plasma protein fragmentation occurs in a time- and HOCl-concentration-dependent manner, as evidenced by the increased mobility of the EPR spin adducts, the detection of further radical species believed to be intermediates in protein degradation and the loss of the parent protein bands on SDS/PAGE. Fragmentation can be inhibited by methionine and other agents (ascorbate, urate, Trolox C or GSH) capable of removing chloramines and reactive radicals. These results are consistent with protein-derived chloramines, and the radicals derived from them, as contributing agents in HOCl-induced plasma protein oxidation.

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