The Molecular Weights and Molecular Weight Heterodispersion of Some Antigens From the Trichloroacetic Acid Soluble Fraction of Human Seminal Plasma

1981 ◽  
Vol 1 (5) ◽  
pp. 266-268
Author(s):  
JOSEFINA M. SCACCIATI DE CEREZO ◽  
ALBERTO S. CEREZO
Keyword(s):  
Molecular Weight ◽  
Seminal Plasma ◽  
Trichloroacetic Acid ◽  
Soluble Fraction ◽  
Human Seminal Plasma ◽  
Molecular Weights

Synthesis and Properties of Uniform Polyisoprene Networks. I. Synthesis and Characterization of α,ω-Dihydroxy-Polyisoprene

1976 ◽  
Vol 49 (2) ◽  
pp. 303-319 ◽  
Author(s):  
M. Morton ◽  
L. J. Fetters ◽  
J. Inomata ◽  
D. C. Rubio ◽  
R. N. Young
Keyword(s):  
Molecular Weight ◽  
Physical Properties ◽  
Soluble Fraction ◽  
Synthesis And Characterization ◽  
Molecular Weights ◽  
Molecular Weight Distributions ◽  
Weight Distributions ◽  
The Subject

Abstract The results of this study are the first to show that high-1,4 linear α,ω-dihydroxypolydienes can be synthesized with (a) predictable molecular weights, (b) narrow molecular weight distributions, and (c) high functionalities. Using the functionalized polyisoprenes prepared in this work, a series of networks was prepared with a purified triisocyanate as the chain linking agent. The soluble fraction in these networks ranged from 4.6 to 1.6 per cent. The characteristics and physical properties of these networks will be the subject of a forthcoming publication.

Effects of short-term high-dose testosterone propionate administration on medium molecular-weight proteins of human seminal plasma

Andrologia ◽  
1994 ◽  
Vol 26 (4) ◽  
pp. 241-245 ◽  
Author(s):  
A. Carpino ◽  
D. Sisci ◽  
S. Aquila ◽  
E. Beraldi ◽  
M. T. Sessa ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Seminal Plasma ◽  
Testosterone Propionate ◽  
High Dose ◽  
Human Seminal Plasma ◽  
Short Term

MOLECULAR WEIGHT AND PHYSICAL PROPERTIES OF A LIPOPROTEIN FROM THE FLOATING FRACTION OF EGG YOLK

1958 ◽  
Vol 36 (1) ◽  
pp. 937-949 ◽  
Author(s):  
K. J. Turner ◽  
W. H. Cook
Keyword(s):  
Molecular Weight ◽  
Sodium Chloride ◽  
Lipid Content ◽  
Soluble Fraction ◽  
Egg Yolk ◽  
Low Molecular Weight ◽  
Molecular Weights ◽  
Ether Extraction ◽  
Soluble Material ◽  
Different Levels

Ether extraction removes 80% of the floating fraction of egg yolk from its solution in 2.5% sodium chloride. On removal of the ether and dialysis against specific solvents two thirds of the remaining lipoprotein (40% lipid) precipitates, leaving a soluble fraction containing 50% lipid. The soluble and insoluble portions probably represent different levels of degradation rather than different lipoproteins since both materials are apparently derived by ether extraction from a natural entity of much higher lipid content. The soluble fraction is heterogeneous and has mean molecular weights of M w = 5.4 × 105by light-scattering methods, and M n = 3.4 × 105by osmotic pressure. A "light" fraction obtained by centrifuging and representing 38% of the soluble material had M w = 3.4 to 3.5 × 105. Heterogeneity in lipid content appears to be responsible for the low molecular weight (M w = 2.4 × 105) obtained by sedimentation.

scholarly journals Gelatinases in Boar Seminal Plasma and Their Relation to Semen Indicators

2010 ◽  
Vol 79 (3) ◽  
pp. 491-496 ◽  
Author(s):  
Maja Zakošek Pipan ◽  
Marjan Kosec ◽  
Janko Mrkun ◽  
Petra Zrimšek
Keyword(s):  
Molecular Weight ◽  
Enzyme Activity ◽  
Seminal Plasma ◽  
Animal Species ◽  
Sperm Concentration ◽  
Gelatin Zymography ◽  
Motile Sperm ◽  
Molecular Weights ◽  
Simultaneous Identification ◽  
First Time

Matrix metalloproteinases were detected in reproductive tissues and seminal plasma of various animal species. The aim of this study was to determine for the first time the presence of gelatinases and metalloproteases in boar seminal plasma and to correlate the results with semen indicators. Gelatin zymography was used for simultaneous identification and measurement of gelatinase enzyme activity associated with their molecular weights. Several gelatinase forms were identified in seminal plasma of boars. Those that were stimulated by CaCl2 and inhibited by EDTA and phenanthroline were considered as metalloproteases. Negative correlation between semen indicators (sperm index, sperm concentration and concentration of progressive motile sperm) and the concentrations of metalloprotease at 78 kDa and 66 kDa means that higher values of semen indicators correlate with lower concentrations of these metaloproteases in seminal plasma. Gelatinases with molecular weight of 225, 78 and 66 kDa correlated with higher levels of acrosome damage. Samples with sperm index above 110 M/ml contained gelatinases of significantly lower band intensities at 78 and 66 kDa compared to samples with SI less than 110 M/ml. Bands with 225, 78 and 66 kDa are suggested to belong to a dimer of MMP-9, proMMP-2 and mature MMP-2.

scholarly journals Purification of plasminogen activators from human seminal plasma

1978 ◽  
Vol 171 (2) ◽  
pp. 435-444 ◽  
Author(s):  
D Propping ◽  
L J D Zaneveld ◽  
P F Tauber ◽  
G F B Schumacher
Keyword(s):  
Seminal Plasma ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Gel Filtration ◽  
Plasminogen Activators ◽  
Exchange Chromatography ◽  
Human Seminal Plasma ◽  
Molecular Weights ◽  
Wide Ph Range

Two plasminogen activators (1 and 2) were isolated from human seminal plasma by hiigh-speed centrifugation, Sephadex-gel filtration and ion-exchange chromatography. The activators were shown to be homogeneous by polyacrylamide-disc -gel electrophoresis at pH 8.3 and 4.5, and by sodium dodecyl sulphate/polyacrylamide-gel electrophoresis. The molecular weights of activators 1 and 2 were estimated as 69 000 and 74 000. Their amino acid compositions are very similar, both being high in aspartic acid, glutamic acid, serine, glycine and leucine, and low in methionine, tryptophan, tyrosine, isoleucine and histidine. Activators 1 and 2 each possess 16 cysteine residues. Both activators have isoelectric points of approx. 7.0, are stable over a wide pH range at temperatures up to 60 degrees C, but lose activity at higher temperatures, particularly under very basic or acidic conditions. They are not inhibited by EDTA, Mg2+ and Ca2+ at 10 mM concentrations, but their activity decreases on addition of 10 mM-cysteine or Fe2+ and 6-aminohexanoate or sera from pregnant women. The precipitin band formed between urokinase and its antiserum is continuous with the precipitin bands formed between the seminal plasminogen activators and the urokinase antiserum. Antisera to urokinase inhibit both the activity of urokinase and the seminal plasminogen activators.

Identification and characterization of a polysaccharide-containing antigen fromSchistosoma mansonieggs which cross-reacts with the surface of schistosomula

Parasitology ◽  
1987 ◽  
Vol 94 (2) ◽  
pp. 255-268 ◽  
Author(s):  
D. W. Dunne ◽  
Q. D. Bickle
Keyword(s):  
Molecular Weight ◽  
Schistosoma Mansoni ◽  
High Molecular Weight ◽  
Concanavalin A ◽  
Trichloroacetic Acid ◽  
Soluble Fraction ◽  
Cell Adherence ◽  
Dependent Cell ◽  
Identification And Characterization

SUMMARYAntisera were produced by immunizing rabbits with either a trichloroacetic acid-soluble fraction, or a high molecular weight (Mr) fraction ofSchistosoma mansoniSEA (a salinesoluble fraction of homogenized egg). Both of these sera reacted monospecifically in immunoelectrophoresis against unfractionated SEA, recognizing a cathodally migrating antigen. This antigen had been identified previously as being responded to byS. mansoni-infected mouse sera, and has been designated K3(Kappa 3). The rabbit antisera were used to partially characterize antigen K3as havingMrin the range > 750 – 70 K, and being resistant to boiling, resistant to the action of proteases, but sensitive to periodate. It partially binds to Concanavalin A. In addition to SEA, the antigen was present in homogenized cercariae and schistosomula, but not adult worms, and it was also present in detergent extracts of intact cercariae and schistosomula. Using an antibody-dependent cell adherence assay, anti-K3serum was found to react with the surface of live cercariae and with the surface of schistosomula recovered from the skin of mice infected up to 48 h previously. Anti-K3serum also reacted with the surface ofS. bovis, S. haematobiumand to a lesser extentS. japonicumschistosomula.

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