scholarly journals Differences in expression density and molecular weight of CR1-Like in erythrocytes of landrace swine

2018 ◽  
Author(s):  
Jingjing Zhang ◽  
Wei Yin ◽  
Chun Wang ◽  
Ruipu Jia ◽  
Kuohai Fan ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Theoretical Data ◽  
Flow Cytometry Analysis ◽  
Immunological Mechanism ◽  
Future Studies ◽  
Molecular Weights ◽  
Immune Adherence ◽  
Sds Page ◽  
Complement Receptor 1 ◽  
Porcine Erythrocyte

Background. Porcine erythrocytes express complement receptor 1-like (CR1-like), which is involved in immune adherence. Methods. In this study, porcine erythrocyte samples were collected from fifty-five individual Landrace swine to characterize differences in porcine CR1-like. Flow cytometry analysis was performed to examine the porcine differences in CR1-like expression density and immunoprecipitation, SDS-PAGE and Western blot were performed to detect variations in porcine CR1-like molecular weights. Results. Different mean fluorescence intensities (MFI) of porcine erythrocytes were identified in three groups as 33.016±2.889 (40.0%), 59.974±9.299 (45.5%) and 131.241±8.375 (14.5%). Under reduced condition, three porcine CR1-like molecular weight variants were identified as 85.280±0.935 kDa (9.09%), 123.939±2.752 kDa (14.55%) and 136.696±2.028 kDa (76.36%). Discussion. CR1-like was dispersed on the surface of porcine erythrocytes and promoted immune adherence. There have been no reports on whether differences in the expression levels and/or molecular weights of CR1-like in erythrocytes represent diversity in different individuals, and if so, whether this diversity influences the immune adherence of erythrocytes and/or whether the diversity is associated with CR1-like polymorphisms. At present, five candidate genes that are related to the differences above were found. Research examining erythrocyte immune adherence and CR1-like genes is under way. These results will provide theoretical data for future studies of the immunological mechanism of CR1-like in porcine erythrocytes.

scholarly journals Differences in expression density and molecular weight of CR1-Like in erythrocytes of landrace swine

2018 ◽  
Author(s):  
Jingjing Zhang ◽  
Wei Yin ◽  
Chun Wang ◽  
Ruipu Jia ◽  
Kuohai Fan ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Theoretical Data ◽  
Flow Cytometry Analysis ◽  
Immunological Mechanism ◽  
Future Studies ◽  
Molecular Weights ◽  
Immune Adherence ◽  
Sds Page ◽  
Complement Receptor 1 ◽  
Porcine Erythrocyte

Background. Porcine erythrocytes express complement receptor 1-like (CR1-like), which is involved in immune adherence. Methods. In this study, porcine erythrocyte samples were collected from fifty-five individual Landrace swine to characterize differences in porcine CR1-like. Flow cytometry analysis was performed to examine the porcine differences in CR1-like expression density and immunoprecipitation, SDS-PAGE and Western blot were performed to detect variations in porcine CR1-like molecular weights. Results. Different mean fluorescence intensities (MFI) of porcine erythrocytes were identified in three groups as 33.016±2.889 (40.0%), 59.974±9.299 (45.5%) and 131.241±8.375 (14.5%). Under reduced condition, three porcine CR1-like molecular weight variants were identified as 85.280±0.935 kDa (9.09%), 123.939±2.752 kDa (14.55%) and 136.696±2.028 kDa (76.36%). Discussion. CR1-like was dispersed on the surface of porcine erythrocytes and promoted immune adherence. There have been no reports on whether differences in the expression levels and/or molecular weights of CR1-like in erythrocytes represent diversity in different individuals, and if so, whether this diversity influences the immune adherence of erythrocytes and/or whether the diversity is associated with CR1-like polymorphisms. At present, five candidate genes that are related to the differences above were found. Research examining erythrocyte immune adherence and CR1-like genes is under way. These results will provide theoretical data for future studies of the immunological mechanism of CR1-like in porcine erythrocytes.

A PLASMINOGEN ACTIVATOR INHIBITOR (PAI-2) CIRCULATES IN TWO HIGH MOLECULAR WEIGHT FORMS IN PREGNANCY

1987 ◽  
Author(s):  
N A Booth ◽  
A Reith ◽  
B Bennett
Keyword(s):  
Molecular Weight ◽  
High Molecular Weight ◽  
Plasminogen Activator ◽  
Apparent Molecular Weight ◽  
Late Pregnancy ◽  
Plasminogen Activator Inhibitor ◽  
Molecular Weights ◽  
Histiocytic Cell ◽  
Sds Page ◽  
Pai 1

Normal vascular endothelium and platelet α-granules contain an inhibitor of plasminogen activator (PAI-1) of about 48000 molecular weight, which is released by stimuli such as thrombin. An immunologically distinct inhibitor (PAI-2) of about 47000 molecular weight has been purified from placenta and from a histiocytic cell line U-937. The level of PA-inhibition in plasma is raised in late pregnancy and this may be due to increases in PAI-1 or in PAI-2 or in both.Using SDS-PAGE and zymography on fibrin/plasminogen /u-PA detector gels, we have found that normal plasma contains a band of inhibition of apparent molecular weight 40000, which can be neutralised by antiserum raised against PAI-1. Pregnancy plasma contained this band as well as additional inhibitor bands of apparent molecular weights 75000 and 130000. The novel high molecular weight PA-inhibitors were detectable by zymography at about 12 weeks gestation. They were specific for plasminogen activator and did not inhibit plasmin. They were inhibited by antiserum raised against PAI-2 from U-937 cells (a gift from Dr EKO Kruithof) and thus are immunologically related to PAI-2. They may represent circulating complexes of PAI-2 with another protein or aggregates of PAI-2, which retain inhibitory activity after SDS-PAGE. PAI-2 appears to represent a pregnancy associated protein that circulates in a number of different molecular weight forms.

Affinity Chromatography of Human Factor VIII Using Human and Rabbit Antibodies to Factor VIII

1979 ◽  
Vol 42 (04) ◽  
pp. 1306-1315 ◽  
Author(s):  
Janet L Lane ◽  
H Ekert ◽  
A Vafiadis
Keyword(s):  
Molecular Weight ◽  
Factor Viii ◽  
Affinity Chromatography ◽  
Protein Concentration ◽  
Gel Filtration ◽  
Subunit Structure ◽  
Molecular Weights ◽  
Human Factor Viii ◽  
Sds Page ◽  
Normal Human

SummaryFactor VIII, purified by gel filtration on Sepharose 2B, has an 8 band multiple subunit structure, with molecular weights ranging from 30,000 to 230,000, on reduction and SDS-PAGE at a protein concentration of 400 μg/gel. Affinity chromatography of this factor VIII preparation with insolubilized haemophilic antibody to factor VIII showed that 45-81% VIII:C and 0-33% VIILRag were attached to the column. Elution of the column with 0.25 M CaCl2 did not show VIII:C or VIILRag in the eluate. NH4SCN dissociation of the column, followed by reduction and SDS-PAGE of the dissociated protein, showed that 95 % of the protein bound by haemophilic antibody had a molecular weight similar to the low molecular weight subunits of the reduced factor VIII.In control experiments with normal Human IgG, 3% of VIII:C and 5% of VIILRag were attached to the column. NH4SCN dissociation of the column, followed by reduction and SDS-PAGE of the protein, showed 2 faint bands with molecular weight consistent with heavy and light chains of IgG.Similar experiments with antibody to factor VIII showed that 67-83% of VIILC and 61-76% of VIII:Rag were attached to the column. Elution of the column with 0.25 M CaCl2 showed 10% of the applied VIII:C, but no VIII:Rag in the eluate. NH4SCN dissociation of the column, followed by reduction and SDS-PAGE of the dissociated protein, showed an 8 band subunit structure similar to the reduced factor VIII.

scholarly journals Production and Characterization of Crude Protease from RS1 Isolate from silage of Floating Bladderwort (Utricularia gibba)

2020 ◽  
Vol 10 (3) ◽  
pp. 289-293
Author(s):  
Ace Baehaki ◽  
Arif Hidayat ◽  
Nuni Gofar ◽  
Rodiana Nopianti
Keyword(s):  
Molecular Weight ◽  
Production Time ◽  
Molecular Weights ◽  
Sds Page ◽  
Optimum Ph ◽  
Utricularia Gibba ◽  
Optimum Production ◽  
Optimum Ph And Temperature

The purpose of this research was to produce and characterizing crude protease from RS1 isolate of swamp plant silage. The optimum production time of RS1 isolate was 40 h. The optimum pH and temperature of protease from RS1 isolate were 10 and 45℃, respectively.  Ion Mg3+ increased RS1 protease whereas ion of Na+, K+, Fe2+, and Zn2+ inhibited protease from RS1 isolate. Study on the effect of metals ion indicated that protease from RS1 isolate was metaloenzyme. Based analysis on SDS-PAGE, the molecular weight of RS1 protease had 12 bands with molecular weights ranging from 34.75 kDa to 263.53 kDa.

scholarly journals Evaluation of urinary proteins in healty full-term neonates by SDS-PAGE

2005 ◽  
Vol 51 ◽  
pp. 9-14
Author(s):  
Snezhana Palchevska ◽  
Velibor Tasik ◽  
Petar Korneti ◽  
Georgi Shestakov ◽  
Svetlana Tsekovska
Keyword(s):  
Molecular Weight ◽  
Full Term ◽  
Urine Samples ◽  
Low Molecular Weight ◽  
Urinary Proteins ◽  
Term Neonates ◽  
Molecular Weights ◽  
Electrophoretic Profile ◽  
Sds Page

The pattern of urinary proteins in healthy full-term neonates was examined by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE), coupled with determination of few parameters related to urinary protein excretion. Twenty healthy full-term neonates were included in the investigation. Five urine samples from each subject were collected on days 3, 7, 14, 21 and 28 after birth. Determination of total proteins was performed using turbidimetric method with sulfosalicylic acid. Urinary creatinine concentration was determined by Jaffe method. Urinary proteins were separated by horizontal gradient SDS-PAGE according to Görg. The highest values for total urinary proteins and for protein/creatinine ratio were detected in urine samples excreted on days 3 and 7 after birth. Three types of SDS-PAG electrophoretic profiles were observed. The first type of electrophoretic profile was characterized by the presence of proteins of mixed glomerular and tubular origin with molecular weights from 10 to 160 kDa. Typical for the second type of electrophoretic profile was the presence of two faint fractions with molecular weights of 78 and 90 kDa and several intensive low molecular weight fractions (14-67 kDa). In the third type of electrophoretic profile only low molecular weight proteins (10-67 kDa) were detected in all five urine samples. These findings express the transitory immaturity of the glomerular filter and tubular protein reabsorbing system of the newborn kidney. Apparently, the tubular protein handling normalizes later than the glomerular filtration of proteins.

scholarly journals Seasonal Variations in Protein Patterns and Mineral Contents of Lycium showii under Different Habitat Conditions

2020 ◽  
pp. 91-103
Author(s):  
Ahmed Mandouh Kamel ◽  
Karima Mohamed El- Absy
Keyword(s):  
Mechanical Properties ◽  
Molecular Weight ◽  
Seasonal Variations ◽  
Habitat Conditions ◽  
Protein Patterns ◽  
Mineral Contents ◽  
Molecular Weights ◽  
Autumn Season ◽  
Sds Page ◽  
South Sinai

Two locations Wadi El-Bagha in South Sinai and Wadi Hashem in Mersa Matruh, Egypt were selected for monitoring changes of protein patterns and chemical composition of Lycium showii (L. showii) due to seasonal variations. Significant differences (P < 0.05 or 0.01) occurred of mechanical properties and chemical analysis of the soil associated of L. showii by 0-20 and 20-40 cm depths from three sites (up, mid, down-streams) in Wadi El-Bagha and Wadi Hashem as well as interactions them (depths, sites and locations). Soil associated with the plants in Wadi Hashem possessed higher water content and electrical conductivity in down-stream as well as higher Cl-, Ca2+, Mg2+, Na+ and K+ in the up-stream during the 20-40 cm depth. Locations, sites and seasons as well as their interactions trends were showed highly significant with plant Na+, K+, Ca2+, Mg2+, N and P contents, with insignificance in Ca2+ and N contents by seasons and locations x seasons, respectively. The Na+ and K+ of Wadi Hashem and N and P of Wadi El-Bagha in autumn as well as Ca2+ of Wadi Hashem and Mg2+ of Wadi El-Bagha in spring were recorded the highest values during mid-stream. The SDS-PAGE method showed different molecular weights of protein patterns in L. shawii leaves in the two locations during autumn and spring seasons. The highest molecular weight (148.3 kD) was observed in Wadi El-Bagha during autumn season, while the lowest molecular weight (10.5 kD) was found in Wadi Hashem and Wadi El-Bagha during spring and autumn season, respectively. The number of bands in Wadi El-Bagha had higher than in Wadi Hashem during the both seasons. The leaves of L. showii have specific unique high molecular weights proteins in Wadi El-Bagha at autumn and spring seasons. Thus, these patterns reflect variations of behavior and adaptation of L. shawii under stress conditions in the studied locations and seasons.    

Variability of Low-Molecular-Weight, Heat-Modifiable Outer Membrane Proteins of Neisseria meningitidis

1980 ◽  
Vol 30 (3) ◽  
pp. 642-648
Author(s):  
J. T. Poolman ◽  
S. De Marie ◽  
H. C. Zanen
Keyword(s):  
Molecular Weight ◽  
Outer Membrane ◽  
High Molecular Weight ◽  
Outer Membrane Proteins ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Low Molecular Weight ◽  
Molecular Weights ◽  
Sds Page ◽  
Index Cases

Analysis of major outer membrane protein (MOMP) profiles of various meningococci by sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis (SDS-PAGE) revealed the presence of 0 to 2 low-molecular-weight, heat-modifiable MOMPs (molecular weight, 25,000 to 32,000) and 1 to 3 high-molecular-weight MOMPs (molecular weight, 32,000 to 46,000). Heat modifiability was investigated by comparing MOMP profiles after heating in SDS solutions at 100°C for 5 min or at 40°C for 1 h. Low-molecular-weight MOMPs shifted to higher apparent molecular weights after being heated at 100°C. Heat modifiability of high-molecular-weight MOMPs varied among strains; whenever modified these proteins shifted to lower apparent molecular weights after complete denaturation. Variability of low-molecular-weight, heat-modifiable MOMPs was demonstrated when MOMP profiles were compared of (i) isolates from index cases and associated cases and carriers among contacts, (ii) different isolates from the same individual, and (iii) isolates from a small epidemic caused by serogroup W-135. In some cases high-molecular-weight MOMPs revealed quantitative differences among related strains. The observed variability and quantitative differences indicate that MOMP serotyping and typing on the basis of SDS-PAGE profiles (PAGE typing) need careful reevaluation.

Gastrin peptide isolation in broiler chicken

2015 ◽  
Author(s):  
A. K. Mandal ◽  
R. K. Das ◽  
A. Maity ◽  
G. R. Sahoo
Keyword(s):  
Molecular Weight ◽  
Broiler Chicken ◽  
Electrophoretic Analysis ◽  
Distilled Water ◽  
Protein Marker ◽  
Molecular Weights ◽  
Sds Page ◽  
Reference Protein ◽  
Relative Molecular Weight

The present study was undertaken to isolate gastrin peptide from the antral tissue of broiler chicken. The chicken antrums, i.e. tissue pieces from a narrow zone at gizzard – duodenal junction were collected, boiled in distilled water, followed by centrifugation at 0° C. The supernatant was collected, added to isopropanol and stirred overnight. After addition of dichloromethane, the aqueous phase was partitioned, aspirated and lyophilized. The electrophoretic analysis (SDS-PAGE) of the antral sample was carried out after running it along with a reference protein marker. Characterization of the antral extract revealed a total of eleven peptide bands having relative molecular weights (Mr) ranging from 4.6 to114.5 kDa, out of which peptides having Mr of 22.6 and 26.3 kDa were major ones. The protein or peptide band showing the lowest relative molecular weight (Mr, 4.6 kDa) was identified as the gastrin.

CHARACTERIZATION OF COLLAGEN EXTRACT FROM THE SKINS OF COMMERCIAL FRESHWATER FISH

2015 ◽  
Vol 77 (33) ◽  
Author(s):  
Anida Aminudin ◽  
Shamsul Muhammad ◽  
Ruhil Hayati Hamdan ◽  
Rumaizi Shaari ◽  
Mariam Firdhaus Mad Nordin ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Freshwater Fish ◽  
Functional Property ◽  
Oreochromis Niloticus ◽  
Clarias Gariepinus ◽  
Cosmetic Products ◽  
Commercial Fish ◽  
Molecular Weights ◽  
Sds Page

Collagen was documented as a difficult and expensive protein to quantify due to its insoluble. It is particularly since solubility is a key functional property in a variety of applications such as healthcare and cosmetic products. The main aim of this study was to extract the collagens from the skins of commercial freshwater fish such as red tilapia (Oreochromis niloticus), catfish (Clarias gariepinus) and pangasius (Pangasius pangasius) together with characteristics defined for each type of collagen extraction. The extracted collagens were determined in their molecular weights by using SDS-PAGE and the structure of it was observed under SEM. The obtained molecular weight of all three commercial fish collagens is approximately >80kDa. The characteristics of each type of collagen were then defined by using appropriate analysis through this research.

scholarly journals Research of camel shanks proteinhydrolyzates by electrophoregram

2021 ◽  
pp. 67-73
Author(s):  
Zh. I. Satayeva ◽  
A. M. Tayeva
Keyword(s):  
Molecular Weight ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Degree Of Hydrolysis ◽  
Favorable Result ◽  
Hydrolysis Time ◽  
Molecular Weights ◽  
Sds Page ◽  
Potential Activity ◽  
Peptide Profiles

This research aims to study the degree of hydrolysis, determining the nature of protein hydrolyzates, which determine their size and molecular weight by the method of electrophoregram. In this research, a camel pancreas suspension was used to hydrolyze proteins from camel shanks. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) was used to monitor the distribution of proteins and evaluate their molecular weights at different incubation times. Electrophoregram processing using the BioCapt program (Vilber Lourmat, France) determines the nature of the hydrolysis of protein and peptide profiles among hydrolyzates and the hydrolysis time for 8 hours shows the most significant accumulation of low molecular weight compounds with a molecular mass of <20 kDa, which is a favorable result for the potential activity of peptides.

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