scholarly journals A Comparative Study of Distribution of Protein and Cholesterol in Various Fractions of Human Semen from Infertile and Fertile Subjects

2012 ◽  
Vol 3 (3) ◽  
pp. 78-82 ◽  
Author(s):  
MS Srinivas ◽  
Vickram Sundaram ◽  
M Ramesh Pathy ◽  
TB Sridharan
Keyword(s):  
Molecular Weight ◽  
Comparative Study ◽  
Seminal Plasma ◽  
Semen Analysis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Human Semen ◽  
Exact Function ◽  
Wide Range ◽  
Significant Difference

ABSTRACT Aim To elucidate the concentration of the protein and cholesterol in different fractions of human semen from different infertile categories and comparing them with the fertile group. Materials and methods The human semen was collected from different infertile categories including oligoasthenospermia, asthenospermia, azoospermia, normospermia, oligospermia and fertile group. Immediately after collection, the semen analysis was done as per WHO standard protocols. After that, the semen was centrifuged to get the different fractions. Four main fractions were obtained, (1) spermatozoa, (2) debris or material that precipitates at 12 K rpm for 10 minutes, (3) prostasomes which was precipitated at 20K rpm for 120 minutes, (4) seminal plasma. The protein concentration was done by Lowry's method and cholesterol was estimated by diagnostic kit. Results Sodium dodecyl sulfate—polyacrylamide gel electrophoresis (SDS PAGE) was run for all the categories of semen samples for their seminal plasma and the fertility associated protein was identified. A significant difference was found in the concentration of proteins in all subfractions when compared between control and infertile categories. Almost 86% of the protein was recovered from soluble fraction. In case of azoospermia, the protein content was very low when compared with fertile group. Seminal plasma proteins were visualized by silver staining. The molecular weight of the protein bands were ranging from 6.5 to 205 kDa. The band with molecular weight around 55 kDa was found to be missing in case of oligoasthenospermia. This particular protein is said to be fertility associated protein. The content of cholesterol for different subfraction of the human semen samples from infertile and fertile samples was compared. A wide range of cholesterol was recovered from prostasomes, that too purified. Conclusion A thrive study have to be done in all the subfractions of the semen irrespective of the category of samples to know the exact function of the each subfractions in terms of protein and cholesterol distribution. How to cite this article Sundaram V, Srinivas MS, Rao KA, Pathy MR, Sridharan TB. A Comparative Study of Distribution of Protein and Cholesterol in Various Fractions of Human Semen from Infertile and Fertile Subjects. Int J Infertility Fetal Med 2012;3(3):78-82.

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.

scholarly journals Assessment of Toxicological Effects of Selected Popular Antidiabetic Drugs in Type II Diabetes Mellitus within Ota, Ogun State, Nigeria

2019 ◽  
pp. 1-10
Author(s):  
Ogunlana Olubanke Olujoke ◽  
Oyebanji Olufisayo Grace ◽  
Ogunlana Oluseyi Ebenezer ◽  
Adekeye Bosede Temitope ◽  
Adeyemi Alaba Oladipupo ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Therapeutic Drug ◽  
Diabetic Patients ◽  
Dietary Control ◽  
Functional Changes ◽  
Ogun State ◽  
Significant Difference ◽  
Liver And Kidney

Aim: The complications associated with diabetes and the new trend of using combination therapy in the management of the disease gave birth to this work, aimed at assessing the hepatotoxic and nephrotoxic effects of selected popularly used antidiabetic medications in type 2 diabetic patients within Ota, Ogun State, Nigeria. Study Design: The participants, diabetic (n=195) and non-diabetic (n=30) were divided into the following groups based on their medications: 1 (Non Diabetic control), 2 (Metformin), 3 (Glimepiride), 4 (Glibenclamide), 5 (Metformin and Glimepiride), 6 (Meformin and Glibenclamide), 7 (Metformin, Glimepiride and Glibenclamide) and 8 (Diabetic Dietary control). Methodology: Serum protein expression profiling, liver and kidney function parameters were assessed in participant’s blood using Sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE) and standard laboratory methods respectively. Results: Glyceamic control within the diabetic groups was 29.23%. Urea concentration was significantly increased (p < 0.05) in groups 5 and 7 compared with groups 1 and 8 while the serum creatinine levels in the different groups showed no significant difference. Activities of alkaline phosphatase and aspartate aminotransferase increased significantly (p < 0.05) in group 5 compared with groups 1 and 8. A low molecular weight protein likely to be Leptin (molecular weight 18 kDa) was over-expressed in all the diabetic groups. Conclusion: This study shows that use of multiple rather than single drugs caused significant functional changes in the liver and kidney. The control of diabetes may best be carried out with dietary control and lifestyle modification as well as good therapeutic drug monitoring for safe assessment of baseline organ function.

scholarly journals Polymerization of proteins with glutaraldehyde. Soluble molecular-weight markers

1973 ◽  
Vol 135 (4) ◽  
pp. 867-873 ◽  
Author(s):  
John W. Payne
Keyword(s):  
Molecular Weight ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Slight Variation ◽  
Protein Markers ◽  
Molecular Weight Range ◽  
Soluble Polymers ◽  
Wide Range ◽  
Weight Protein ◽  
Covalently Linked

Glutaraldehyde is well known for its ability to react with proteins and to produce insoluble cross-linked aggregates. In contrast with this situation, conditions are described here which yield covalently linked soluble protein oligomers. The procedure is applicable to a wide range of proteins, and by slight variation in the reaction conditions, soluble polymers in the molecular weight range 3×104−2×107were produced. The products are valuable aṡ molecular-weight markers, e.g. in sodium dodecyl sulphate–polyacrylamide-gel electrophoresis. The inherent similarities of these oligomers make them superior to commercial molecular-weight protein markers, which may have marked differences in composition and charge.

scholarly journals Genetic Diversity of High and Low Molecular Weight Glutenin Subunits in Algerian Aegilops geniculata

2014 ◽  
Vol 42 (2) ◽  
pp. 453-459 ◽  
Author(s):  
Asma MEDOURI ◽  
Inès BELLIL ◽  
Douadi KHELIFI
Keyword(s):  
Molecular Weight ◽  
High Molecular Weight ◽  
Storage Proteins ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Low Molecular Weight ◽  
Glutenin Subunits ◽  
Bread Making ◽  
Aegilops Geniculata ◽  
Wide Range

Aegilops geniculata Roth is an annual grass relative to cultivated wheat and is widely distributed in North Algeria. Endosperm storage proteins of wheat and its relatives, namely glutenins and gliadins, play an important role in dough properties and bread making quality. In the present study, the different alleles encoded at the four glutenin loci (Glu-M1, Glu-U1, Glu-M3 and Glu-U3) were identified from thirty five accessions of the tetraploid wild wheat A. geniculata collected in Algeria using Sodium dodecyl Sulfate - Polyacrylamide Gel Electrophoresis (SDS-PAGE). At Glu-M1 and Glu-U1 loci, encoding high molecular weight glutenin subunits (HMW-GS) or A-subunits, 15 and 12 alleles were observed respectively, including one new subunit. B-Low molecular weight glutenin subunits zone (B-LMW-GS) displayed a far greater variation, as 28 and 25 alleles were identified at loci Glu-M3 and Glu-U3 respectively. Thirty two subunits patterns were revealed at the C subunits- zone and a total of thirty four patterns resulted from the genetic combination of the two zones (B- and C-zone). The wide range of glutenin subunits variation (high molecular weight glutenin subunits and low molecular weight glutenin subunits) in this species has the potential to enhance the genetic variability for improving the quality of wheat./span>

scholarly journals Oxidation of polymines by diamine oxidase from human seminal plasma

1975 ◽  
Vol 145 (2) ◽  
pp. 373-378 ◽  
Author(s):  
E Hölttä ◽  
P Pulkkinen ◽  
K Elfving ◽  
J Jänne
Keyword(s):  
Molecular Weight ◽  
Seminal Plasma ◽  
Gel Electrophoresis ◽  
Diamine Oxidase ◽  
Polyacrylamide Gel Electrophoresis ◽  
Polyacrylamide Gel ◽  
Human Semen ◽  
Human Seminal Plasma ◽  
Ph Values

1. Diamine oxidase [amine-oxygen oxidoreductase (deaminating)(pyridoxal-containing), EC 1.4.3.6] was purified from human seminal plasma more than 1,700-fold. The enzyme appeared to be homogeneous on polyacrylamide-gel electrophoresis at two different pH values. 2. The general properties of the enzyme were comparable with those described for other diamine oxidases from different mammalian sources. The molecular weight of the enzyme was calculated to be about 182,000. 3. The enzyme had highest affinity for diamines, but polyamines spermidine and spermine were also degraded at concentrations that can be considered physiological in human semen. 3. The possible degradation of spermine by diamine oxidase in human semen in vivo may give rise to the formation of cytotoxic aldehydes that conceivably can influence the motility and survival of the spermatozoa.

Heterozygous Abnormal Fibrinogen Osaka III with the Replacement of γ Arginine-275 by Histidine Has an Apparently Higher Molecular Weight γ-Chain Variant

1992 ◽  
Vol 68 (05) ◽  
pp. 534-538 ◽  
Author(s):  
Nobuhiko Yoshida ◽  
Shingi Imaoka ◽  
Hajime Hirata ◽  
Michio Matsuda ◽  
Shinji Asakura
Keyword(s):  
Molecular Weight ◽  
Sodium Dodecyl Sulfate ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Tetraacetic Acid ◽  
Fibrin Monomer ◽  
Sds Page ◽  
Thrombotic Tendency ◽  
Chain Variant

SummaryCongenitally abnormal fibrinogen Osaka III with the replacement of γ Arg-275 by His was found in a 38-year-old female with no bleeding or thrombotic tendency. Release of fibrinopeptide(s) by thrombin or reptilase was normal, but her thrombin or reptilase time in the absence of calcium was markedly prolonged and the polymerization of preformed fibrin monomer which was prepared by the treatment of fibrinogen with thrombin or reptilase was also markedly defective. Propositus' fibrinogen had normal crosslinking abilities of α- and γ-chains. Analysis of fibrinogen chains on sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) in the system of Laemmli only revealed the presence of abnormal γ-chain with an apparently higher molecular weight, the presence of which was more clearly detected with SDS-PAGE of fibrin monomer obtained by thrombin treatment. Purified fragment D1 of fibrinogen Osaka III also seemed to contain an apparently higher molecular weight fragment D1 γ remnant on Laemmli gels, which was digested faster than the normal control by plasmin in the presence of [ethy-lenebis(oxyethylenenitrilo)]tetraacetic acid (EGTA).

scholarly journals Biochemical and molecular characterization of Alternaria alternata isolates highly resistant to procymidone from broccoli and cabbage

2021 ◽  
Vol 3 (1) ◽  
Author(s):  
Bingran Wang ◽  
Tiancheng Lou ◽  
Lingling Wei ◽  
Wenchan Chen ◽  
Longbing Huang ◽  
...  
Keyword(s):  
Alternaria Alternata ◽  
Single Point ◽  
Sodium Dodecyl ◽  
Cross Resistance ◽  
Molecular Characteristics ◽  
Single Point Mutation ◽  
Wide Range ◽  
Significant Difference ◽  
Leaf Blights ◽  
High Level

AbstractAlternaria alternata, a causal agent of leaf blights and spots on a wide range of hosts, has a high risk of developing resistance to fungicides. Procymidone, a dicarboximide fungicide (DCF), has been widely used in controlling Alternaria leaf blights in China for decades. However, the resistance of A. alternata against DCFs has rarely been reported from crucifer plants. A total of 198 A. alternata isolates were collected from commercial fields of broccoli and cabbage during 2018–2019, and their sensitivities to procymidone were determined. Biochemical and molecular characteristics were subsequently compared between the high-level procymidone-resistant (ProHR) and procymidone-sensitive (ProS) isolates, and also between ProHR isolates from broccoli and cabbage. Compared with ProS isolates, the mycelial growth rate, sporulation capacity and virulence of most ProHR isolates were reduced; ProHR isolates displayed an increased sensitivity to osmotic stresses and a reduced sensitivity to sodium dodecyl sulfate (SDS); all ProHR isolates showed a reduced sensitivity to hydrogen peroxide (H2O2) except for the isolate B102. Correlation analysis revealed a positive cross-resistance between procymidone and iprodione, or fludioxonil. When treated with 10 μg/mL of procymidone, both mycelial intracellular glycerol accumulations (MIGAs) and relative expression of AaHK1 in ProS isolates were higher than those in ProHR isolates. Sequence alignment of AaHK1 from ten ProHR isolates demonstrated that five of them possessed a single-point mutation (P94A, V612L, E708K or Q924STOP), and four isolates had an insertion or a deletion in their coding regions. No significant difference in biochemical characteristics was observed among ProHR isolates from two different hosts, though mutations in AaHK1 of the cabbage-originated ProHR isolates were distinct from those of the broccoli-originated ProHR isolates.

scholarly journals A comparative study on the extraction effects of common agents on collagen-based binders in mural paintings

2021 ◽  
Vol 9 (1) ◽  
Author(s):  
Jianghao Du ◽  
Zhanyun Zhu ◽  
Junchang Yang ◽  
Jia Wang ◽  
Xiaotong Jiang
Keyword(s):  
Protein Structure ◽  
Comparative Study ◽  
Protein Extraction ◽  
Guanidine Hydrochloride ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Extraction Process ◽  
Ultraviolet Absorption Spectrum ◽  
Mural Paintings ◽  
The Impact

AbstractIn this paper, a comparative study was conducted on the extraction effects of six agents for collagen-based mural painting binders. These agents were used to extract the residual proteins in the non-aged and thermal aged samples. The protein extraction efficiencies of different extracting agents were quantitatively determined by bicinchoninic acid (BCA) method, and then processed by multivariate analysis of variance (MANOVA). The impact of the extraction process on the protein structure was characterized by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE), ultraviolet absorption spectrum (UV) and circular dichroism (CD). The results showed that, for both non-aged and aged samples, the extraction efficiency of 2 M guanidine hydrochloride (GuHCl) was significantly higher than the other five agents, with less damage to the protein structure during the extraction process.

Purification and partial characterization of cysteine-glutamate transaminase from rat liver

1977 ◽  
Vol 55 (9) ◽  
pp. 958-964 ◽  
Author(s):  
M. P. C. Ip ◽  
R. J. Thibert ◽  
D. E. Schmidt Jr.
Keyword(s):  
Molecular Weight ◽  
Rat Liver ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Liver Homogenate ◽  
Polyacrylamide Gel ◽  
Gel Chromatography ◽  
Labile Hydrogen ◽  
Apparent Homogeneity

Cysteine-glutamate transaminase (cysteine aminotransferase; EC 2.6.1.3) has been purified 149-fold to an apparent homogeneity giving a specific activity of 2.09 IU per milligram of protein with an overall yield of 15%. The isolation procedures involve the preliminary separation of a crude rat liver homogenate which was submitted sequentially to ammonium sulfate fractionation, TEAE-cellulose column chromatography, ultrafiltration, and isoelectrofocusing. The final product was homogenous when examined by polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate (SDS). A minimal molecular weight of 83 500 was determined by Sephadex gel chromatography. The molecular weight as estimated by polyacrylamide gel electrophoresis in the presence of SDS was 84 000. The purified enzyme exhibited a pH optimum at 8.2 with cysteine and α-ketoglutarate as substrates. The enzyme is inactivated slowly when kept frozen and is completely inactivated if left at room temperature for 1 h. The enzyme does not catalyze the transamination of α-methyl-DL-cysteine, which, when present to a final concentration of 10 mM, exhibits a 23.2% inhibition of transamination of 30 mM of cysteine. The mechanism apparently resembles that of aspartate-glutamate transaminase (EC 2.6.1.1) in which the presence of a labile hydrogen on the alpha-carbon in the substrate is one of the strict requirements.

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