Еffect of different breeds on the protein profile in ram seminal plasma

2021 ◽  
Vol 24 (3) ◽  
pp. 344-354
Author(s):  
M. Ivanova ◽  
D. Gradinarska ◽  
S. Yotov ◽  
D. Abadjieva ◽  
Ts. Tzvetkov ◽  
...  
Keyword(s):  
Seminal Plasma ◽  
Protein Profile ◽  
Polyacrylamide Gel Electrophoresis ◽  
Biological Marker ◽  
Sds Page ◽  
Specific Proteins ◽  
Molecular Masses ◽  
Seminal Plasma Proteins ◽  
The Individual ◽  
Individual Profiles

In this study the individual profiles of seminal plasma proteins (SPP) in rams of three breeds – Merino, Pleven Blackhead and Ile de France - were analysed. The study was carried out with three rams at 3, 6 and 10 years of age, grown and fed under similar conditions. Eighteen ejaculates (6 ejaculates from each ram) were evaluated by Sperm Class Analyzer. The total SPP concentration was measured spectrophotometrically. The separation and characterisation of SPP was performed by HPLC and one dimensional polyacrylamide gel electrophoresis (SDS-PAGE). There were no significant differences between the characteristics of ejaculates and the main kinematic parameters of the sperm in the breeds studied. Chromatograms showed specific profiles with 9, 10 and 11 protein peaks for Merino, Pleven Blackhead and Ile de France breeds, respectively. The total SPP concentration was the highest in the Pleven Blackhead breed and the lowest in Ile de France breed. The major parts of SPP in the three breeds were identical. The seminal plasma of Merino breed contained proteins with molecular mass of 30.3 kDa, 15.7 kDa and 15.2 kDa that were not present in the other two breeds. In the Ile de France and Pleven Blackhead samples only, two proteins with molecular masses of 39.7 kDa and 21.1 kDa, were observed. In conclusion, the detection of specific proteins can be used as a biological marker for sheep breed identification.

scholarly journals The Oligomeric State of c Rings from Cyanobacterial F-ATP Synthases Varies from 13 to 15

2007 ◽  
Vol 189 (16) ◽  
pp. 5895-5902 ◽  
Author(s):  
Denys Pogoryelov ◽  
Christian Reichen ◽  
Adriana L. Klyszejko ◽  
René Brunisholz ◽  
Daniel J. Muller ◽  
...  
Keyword(s):  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Environmental Groups ◽  
Oligomeric State ◽  
Sds Page ◽  
C Subunit ◽  
Molecular Masses ◽  
The Individual ◽  
The Masses ◽  
Atp Synthases

ABSTRACT We isolated the c rings of F-ATP synthases from eight cyanobacterial strains belonging to four different taxonomic classes (Chroococcales, Nostocales, Oscillatoriales, and Gloeobacteria). These c rings showed different mobilities on sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), probably reflecting their molecular masses. This supposition was validated with the previously characterized c11, c14, and c15 rings, which migrated on SDS-PAGE in proportion to their molecular masses. Hence, the masses of the cyanobacterial c rings can conveniently be deduced from their electrophoretic mobilities and, together with the masses of the c monomers, allow the calculation of the c ring stoichiometries. The method is a simple and fast way to determine stoichiometries of SDS-stable c rings and hence a convenient means to unambiguously determine the ion-to-ATP ratio, a parameter reflecting the bioenergetic efficacy of F-ATP synthases. AFM imaging was used to prove the accuracy of the method and confirmed that the c ring of Synechococcus elongatus SAG 89.79 is a tridecameric oligomer. Despite the high conservation of the c-subunit sequences from cyanobacterial strains from various environmental groups, the stoichiometries of their c rings varied between c13 and c15. This systematic study of the c-ring stoichiometries suggests that variability of c-ring sizes might represent an adaptation of the individual cyanobacterial species to their particular environmental and physiological conditions. Furthermore, the two new examples of c15 rings underline once more that an F1/Fo symmetry mismatch is not an obligatory feature of all F-ATP synthases.

scholarly journals Comparative evaluation of seminal plasma proteins in Holsteiner and East Bulgarian horse breeds in relation to functional parameters of spermatozoa

2021 ◽  
Vol 24 (3) ◽  
pp. 355-364
Author(s):  
M. G. Ivanova ◽  
B. A. Georgiev ◽  
P. S. Taushanova ◽  
D. G. Gradinarska ◽  
T. S. Tsvetkov ◽  
...  
Keyword(s):  
Seminal Plasma ◽  
Protein Profile ◽  
Specific Protein ◽  
Sperm Head ◽  
Kinematic Parameters ◽  
Protein Mass ◽  
Specific Proteins ◽  
Chromatographic Peaks ◽  
The Individual ◽  
Head Area

The present research was focused on the differentiation of specific proteins in the seminal plasma (SP) of two horse breeds - Holsteiner (n=4) and East Bulgarian (n=4) and their relation with indivi­dual or breed characteristics, kinematic parameters of spermatozoa and the sperm head area. After CASA analysis of 8 ejaculates, no statistical differences in the kinematic parameters of the sperms between the two horse breeds were found out with the exception of the sperm head area (P<0.05), which can be considered as a morphometric marker of breed affiliation. The values ​​for rapid sperm in East Bulgarian and Holsteiners were 28.1±0.2 μm2 and 19.9±0.3 μm2 respectively. The chromatographic analysis demonstrated specific quantitative and qualitative protein content of the individual chromatographic peaks (11 for Holsteiner and 15 for the Eastern Bulgarian breed), with similarity to the basic proteins. Three specific proteins with a molecular mass of 76 kDa, 21.6 kDa and 24.3 kDa, were differentiated by SDS PAGE in the Holsteiner breed, whereas in the Eastern Bulgarian horse breed they had a lower protein mass - 30.1 kDa and 14.2 kDa and 12.6 kDa. In conclusion, differences in the specific protein profile of Holsteiner and Eastern Bulgarian horse breeds are individually and naturally determined without significant effect on sperm kinematics. The sperm head area was a breed-specific difference.

The nature and significance of multiple isoforms of the oestrogen receptor in breast tumours

1993 ◽  
Vol 11 (1) ◽  
pp. 83-90 ◽  
Author(s):  
J R Puddefoot ◽  
V A Baker ◽  
B Bakkers ◽  
S Marsigliante ◽  
S Barker ◽  
...  
Keyword(s):  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Progesterone Receptors ◽  
Breast Tumours ◽  
Sds Page ◽  
Isoelectric Points ◽  
Molecular Masses ◽  
The Individual ◽  
Gradient Fractionation ◽  
Tamoxifen Aziridine

ABSTRACT Oestrogen receptors (ERs) in breast tumours are highly heterogeneous. In previous studies we have shown that at least four isoforms may exist. These migrate in isoelectric focusing (IEF) gels to isoelectric points (pI values) 6·1, 6·3, 6·6 and 6·8. Of these the first (pI 6·1) corresponds to the 8S isoform as detected by sucrose gradient fractionation, while the others all sediment at 4S. In a series of 66 breast tumours it was found that those at pI 6·3 and pI 6·8 were significantly correlated with the presence of progesterone receptors. To characterize the isoforms more fully, ER isoforms labelled by [3H]oestradiol binding were fractionated by IEF. The results were compared with those obtained after sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE) and immunoblotting using the H222 anti-ER monoclonal antibody. In other experiments, tumour ER isoforms were covalently labelled with [ring-3H] tamoxifen aziridine and separated by IEF. The individual isoforms were electroeluted from the IEF gel and further analysed by SDS-PAGE and non-denaturing PAGE. In summary, the evidence shows that the isoforms of pI values 6·3, 6·8 and 6·6 have molecular masses of 50, 65 and 70 kDa respectively. In addition, all three of these isoforms, i.e. the pI 6·3, 6·8 and 6·6 isoforms, could form dimers. We conclude that the three isoforms sedimenting at 4S have the capacity to form dimers and thus may have the potential for binding to oestrogen response elements in the genome.

Two-dimensional polyacrylamide gel electrophoresis map of bull seminal plasma proteins

1998 ◽  
Vol 19 (5) ◽  
pp. 797-801 ◽  
Author(s):  
Michele Mortarino ◽  
Gabriella Tedeschi ◽  
Armando Negri ◽  
Fabrizio Ceciliani ◽  
Luciano Gottardi ◽  
...  
Keyword(s):  
Seminal Plasma ◽  
Gel Electrophoresis ◽  
Plasma Proteins ◽  
Polyacrylamide Gel Electrophoresis ◽  
Polyacrylamide Gel ◽  
Two Dimensional ◽  
Seminal Plasma Proteins

Protein Expression in Vibrio parahaemolyticus 690 Subjected to Sublethal Heat and Ethanol Shock Treatments

2008 ◽  
Vol 71 (11) ◽  
pp. 2289-2294 ◽  
Author(s):  
MING-LUN CHIANG ◽  
WEI-LI HO ◽  
ROCH-CHUI YU ◽  
CHENG-CHUN CHOU
Keyword(s):  
Heat Shock ◽  
Vibrio Parahaemolyticus ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Test Organism ◽  
Protein Patterns ◽  
One Dimensional ◽  
Sds Page ◽  
Molecular Masses ◽  
Stressed Cells

Cells of Vibrio parahaemolyticus 690 were subjected either to heat shock at 42°C for 45 min or to ethanol shock in the presence of 5% ethanol for 60 min. The protein profiles of the unstressed and stressed V. parahaemolyticus cells were compared. Additionally, the induction of DnaK- and GroEL-like proteins in the unstressed and stressed cells of V. parahaemolyticus was also examined. Analysis with one-dimensional sodium dodecyl sulfate–polyacrylamide gel electrophoresis (SDS-PAGE) indicated that three proteins with molecular masses of 93, 77, and 58 kDa were induced by both heat shock and ethanol shock. The protein patterns revealed by two-dimensional electrophoresis were more detailed than those revealed by one-dimensional SDS-PAGE. It was found that heat shock and ethanol shock affected the expression of a total of 28 proteins. Among them, four proteins with molecular masses of 94, 32.1, 26.7, and 25.7 kDa were enhanced by both heat shock and ethanol shock. Furthermore, immunoblot analysis showed the presence of a GroEL-like protein with a molecular mass of 61 kDa in the test organism, with the heat-shocked and ethanol-shocked cells producing a GroEL-like protein in a larger quantity than the unstressed cells. However, DnaK-like protein was not detectable in either the unstressed or the stressed cells.

scholarly journals  Analysis of whole cell protein profiles of Salmonella serovars isolated from chicken, turkey and sheep faeces by SDS-PAGE

2010 ◽  
Vol 55 (No. 6) ◽  
pp. 259-263 ◽  
Author(s):  
A. Aksakal
Keyword(s):  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Visual Assessment ◽  
Cell Protein ◽  
Protein Profiles ◽  
Whole Cell ◽  
Sds Page ◽  
Molecular Masses ◽  
Whole Cell Protein ◽  
Salmonella Serovars

This study was carried out to determine the whole cell protein profiles of Salmonella serovars from chicken, turkey and sheep faeces by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). A total of 34 Salmonella strains were included in the study, 14 of them were isolated from chicken, 14 from turkey and six from sheep. SDS-PAGE was carried out using 12% (w/v) separating and 4% (w/v) stacking gels. The results showed more than 30 protein bands ranging in size from 97 kDa (kilodaltons) to below 14.4 kDa as determined by visual assessment of their approximate molecular masses. Protein bands of 78.1, 51.2, 41.5, 37.3, 35.1, 33.9, 30.7, 27.6, 25.4, and 24 kDa were detected in all Salmonella serovars. Salmonella strains used in this study were closely related and could not be differentiated depending on the whole cell protein profiles using SDS-PAGE.

Monthly variations in ovine seminal plasma proteins analyzed by two-dimensional polyacrylamide gel electrophoresis

2006 ◽  
Vol 66 (4) ◽  
pp. 841-850 ◽  
Author(s):  
J.A. Cardozo ◽  
M. Fernández-Juan ◽  
F. Forcada ◽  
A. Abecia ◽  
T. Muiño-Blanco ◽  
...  
Keyword(s):  
Seminal Plasma ◽  
Gel Electrophoresis ◽  
Plasma Proteins ◽  
Polyacrylamide Gel Electrophoresis ◽  
Polyacrylamide Gel ◽  
Two Dimensional ◽  
Seminal Plasma Proteins ◽  
Monthly Variations

Heparin Binding Proteins of Black Bengal Buck Semen and Their Correlation with Sperm Characters and Freezability

2019 ◽  
Author(s):  
M Karunakaran ◽  
Vivek C Gajare ◽  
Ajoy Mandal ◽  
Mohan Mondal ◽  
S K Das ◽  
...  
Keyword(s):  
Seminal Plasma ◽  
Binding Proteins ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Heparin Binding ◽  
Sds Page ◽  
Significant Difference ◽  
Sperm Characters

This experiment was conducted to study the electrophoretic characters of heparin binding proteins (HBP) of Black Bengal buck semen and their correlation with sperm characters and cryo-survivability. Semen ejaculates (n=20/buck) were collected from nine bucks and in vitro sperm characters were evaluated at collection, after equilibration and after freeze - thawing. HBP were isolated through heparin column and discontinuous Sodium Dodecyl Sulphate Polyacrylamide Gel Electrophoresis (SDS-PAGE) was performed to assess molecular weight. Significant difference (plessthan0.01) were observed among the bucks in sperm characters and freezability. Eight protein bands of 17 to 180 kDa in seminal plasma and 7 bands in sperm were found. 180 -136 kDa HBP of seminal plasma and 134-101 kDa HBP of sperm had showed high correlation with in vitro sperm characters. Further studies on identification of these proteins and their correlation with in vivo pregnancy are needed to find their role as marker for buck selection.

A rapid method of species identification of wild chironomids (Diptera: Chironomidae) via electrophoresis of hemoglobin proteins in sodium dodecyl sulfate polyacrylamide gel (SDS–PAGE)

2014 ◽  
Vol 104 (5) ◽  
pp. 639-651 ◽  
Author(s):  
J.T. Oh ◽  
J.H. Epler ◽  
C.S. Bentivegna
Keyword(s):  
Sodium Dodecyl Sulfate ◽  
Protein Profile ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Head Capsule ◽  
Species Level ◽  
Polyacrylamide Gel ◽  
Taxonomic Identification ◽  
Sds Page ◽  
Dodecyl Sulfate

AbstractStudying aquatic benthic macroinvertebrates (BMIs) in the field requires accurate taxonomic identification, which can be difficult and time consuming. Conventionally, head capsule morphology has been used to identify wild larvae of Chironomidae. However, due to the number of species and possible damage and/or deformity of their head capsules, another supporting approach for identification is needed. Here, we provide hemoglobin (Hb) protein in hemolymph of chironomids as a new biomarker that may help resolve some of the ambiguities and difficulties encountered during taxonomic identification. Chironomids collected from two locations in Maine and New Jersey, USA were identified to the genus level and in some cases to the species-level using head capsule and body morphologies. The head capsule for a particular individual was then associated with a corresponding Hb protein profile generated from sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS–PAGE). Distinct Hb profiles were observed from one group (Thienemannimyia) and four genera (Chironomus, Cricotopus, Dicrotendipes, and Glyptotendipes) of chironomids. Several species were polymorphic, having more than one Hb profile and/or having bands of the same size as those of other species. However, major bands and the combination of bands could distinguish individuals at the genus and sometimes species-level. Overall, this study showed that Hb profiles can be used in combination with head capsule morphology to identify wild chironomids.

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