Semen variables and sperm membrane protein profile of Saanen bucks (Capra hircus) in dry and rainy seasons of the northeastern Brazil (3°S)

2014 ◽  
Vol 59 (5) ◽  
pp. 561-573 ◽  
Author(s):  
M. F. van Tilburg ◽  
M. G. F. Salles ◽  
M. M. Silva ◽  
R. A. Moreira ◽  
F. B. Moreno ◽  
...  
Keyword(s):  
Membrane Protein ◽  
Protein Profile ◽  
Northeastern Brazil ◽  
Capra Hircus ◽  
Sperm Membrane ◽  
Dry And Rainy Seasons

Partial purification of a boar sperm membrane protein inducing sperm agglutinating antibody

1990 ◽  
Vol 10 (2) ◽  
pp. 131-139
Author(s):  
Oyewole Adeyemo ◽  
E. O. Okegbile ◽  
O. O. Olorunsogo
Keyword(s):  
Molecular Weight ◽  
Membrane Protein ◽  
Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Gel Filtration ◽  
Partial Purification ◽  
Boar Sperm ◽  
Sperm Membrane ◽  
Triton X

For the development of immunological contraception, attention is being concentrated on the possibility of using a sperm membrane antigen. Boar sperm membrane was extracted with triton-X 100 and fractionated by Sephadex G-150 column chromatography. The glycosylated and nonglycosylated portions of protein peaks from the gel filtration were obtained by fractionating on concanavalin A-Sepharose and eluting the bound protein with 0.3 M methyl mannoside. A glycosylated fraction was found to induce sperm agglutinating antibodies in rabbit. The partially purified protein has a molecular weight of 30 kilodaltons, as determined by sodium dodecyl polyaccyrlamide gel electrophoresis. Further work is planned on the histochemical determination of the origin of this protein and species cross-activity of the antibody.

scholarly journals Temporal variation of the phytoplankton community at short sampling intervals in the Mundaú reservoir, Northeastern Brazil

2008 ◽  
Vol 22 (4) ◽  
pp. 970-982 ◽  
Author(s):  
Ênio Wocyli Dantas ◽  
Ariadne do Nascimento Moura ◽  
Maria do Carmo Bittencourt-Oliveira ◽  
João Dias de Toledo Arruda Neto ◽  
Airlton de Deus C. Cavalcanti
Keyword(s):  
Phytoplankton Community ◽  
Abiotic Factors ◽  
Distribution Patterns ◽  
Northeastern Brazil ◽  
Cylindrospermopsis Raciborskii ◽  
Algae Biomass ◽  
Dissolved Phosphorus ◽  
Sampling Intervals ◽  
Abiotic Variables ◽  
Dry And Rainy Seasons

The aim of this study was to determine how abiotic factors drive the phytoplankton community in a water supply reservoir within short sampling intervals. Samples were collected at the subsurface (0.1 m) and bottom of limnetic (8 m) and littoral (2 m) zones in both the dry and rainy seasons. The following abiotic variables were analyzed: water temperature, dissolved oxygen, electrical conductivity, total dissolved solids, turbidity, pH, total nitrogen, nitrite, nitrate, total phosphorus, total dissolved phosphorus and orthophosphate. Phytoplankton biomass was determined from biovolume values. The role abiotic variables play in the dynamics of phytoplankton species was determined by means of Canonical Correspondence Analysis. Algae biomass ranged from 1.17×10(4) to 9.21×10(4) µg.L-1; cyanobacteria had biomass values ranging from 1.07×10(4) to 8.21×10(4) µg.L-1. High availability of phosphorous, nitrogen limitation, alkaline pH and thermal stability all favored cyanobacteria blooms, particularly during the dry season. Temperature, pH, total phosphorous and turbidity were key factors in characterizing the phytoplankton community between sampling times and stations. Of the species studied, Cylindrospermopsis raciborskii populations were dominant in the phytoplankton in both the dry and rainy seasons. We conclude that the phytoplankton was strongly influenced by abiotic variables, particularly in relation to seasonal distribution patterns.

scholarly journals Adición de proteínas del plasma seminal ovino durante la congelación del espermatozoide y efectos sobre su motilidad y viabilidad

2009 ◽  
Vol 10 (1) ◽  
pp. 51 ◽  
Author(s):  
Jaime Antonio Cardozo ◽  
Patricia Grasa ◽  
María Teresa Muiño B. ◽  
José Álvaro Cebrián P.
Keyword(s):  
Membrane Protein ◽  
Sperm Motility ◽  
Seminal Plasma ◽  
Gel Electrophoresis ◽  
Plasma Proteins ◽  
Two Dimensional ◽  
Plasma Séminal ◽  
Sperm Membrane ◽  
Seminal Plasma Proteins ◽  
Ram Sperm

<p>Este estudio se adelantó para evaluar el efecto de la adición de proteínas del plasma seminal de cordero en la criopreservación sobre la motilidad e integridad de la membrana espermática, y los cambios en el perfil electroforético de las proteínas de la membrana espermática inducidos por la criopreservación. Se usaron eyaculados de ocho corderos adultos de la raza rasa aragonesa, se les determinó su viabilidad y motilidad espermáticas y posteriormente se sometieron a un procedimiento de congelación. Las proteínas se separaron por el método de electroforesis en geles de acrilamida en dos dimensiones. Se obtuvo un mejoramiento significativo (<em>p </em>&lt; 0,05) en la calidad del semen congelado, cuando se adicionaron proteínas del plasma seminal. El análisis bidimensional comparativo entre el semen fresco y el congelado evidenció la pérdida de 8 puntos de proteína en el espermatozoide descongelado. La concentración de un punto de proteína de membrana espermática, de bajo peso molecular (punto 2), fue más alta (<em>p </em>&lt; 0,05) en el espermatozoide descongelado al que se adicionaron proteínas del plasma seminal. Se encontraron correlaciones entre algunos puntos de proteína y la motilidad y viabilidad espermáticas, lo cual sugiere que pueden jugar papeles importantes en el mantenimiento de la integridad y funcionalidad del espermatozoide. Se puede concluir que la adición de proteínas del plasma seminal en la congelación mejora la integridad del espermatozoide descongelado, y que la criopreservación del semen de cordero produce variaciones en la composición de las proteínas de membrana.  </p><p> </p><p><strong>Effect of seminal plasma proteins at freezing on ram sperm motility and viability</strong>  </p><p>The aim of the study was to evaluate the cryoprotective effect of seminal plasma proteins on ram sperm motility, membrane integrity and the changes in the profile of ram sperm membrane proteins induced by cryopreservation. Fresh ejaculates from 8 mature Rasa aragonesa rams were used. Sperm motility and cell viability was assessed. The freezing procedure was based on the method described by Fiser <em>et al</em>. (1987). Proteins extracted from fresh and frozen-thawed semen were subjected to the Two-dimensional polyacrilamide gel electrophoresis. A significant improvement in the quality of frozenthawed sperm was obtained after addition of seminal plasma proteins (<em>p </em>&lt; 0.05). Comparative two-dimensional polyacrilamide gel electrophoresis analysis between fresh and frozen semen, either with or without seminal plasma proteins in the cryopreservation medium, revealed that eight protein spots were lost in frozen-thawed sperm. The concentration of one sperm membrane protein spot of low Mr (spot 2) was higher (<em>p </em>&lt; 0.05) in proteinadded frozen sperm. Correlations found between certain protein spots sperm motility and viability suggests that these proteins could play important roles in the maintenance of sperm integrity and functionality. In conclusion, the addition of seminal plasma proteins to freezing extender improved frozen-thawed ram sperm integrity quality and cryopreservation of ram semen produced variations in the sperm membrane protein composition. </p>

Growth phase-dependent variations in the outer membrane protein profile of Brucella melitensis

1995 ◽  
Vol 146 (3) ◽  
pp. 227-236 ◽  
Author(s):  
T Gallot-Lavallée ◽  
M.S Zygmunt ◽  
A Cloeckaert ◽  
G Bézard ◽  
G Dubray
Keyword(s):  
Membrane Protein ◽  
Outer Membrane ◽  
Growth Phase ◽  
Outer Membrane Protein ◽  
Brucella Melitensis ◽  
Protein Profile

Sperm membrane protein (hSMP-1) and RanBPM complex in the microtubule-organizing centre

2004 ◽  
Vol 82 (6) ◽  
pp. 383-388 ◽  
Author(s):  
Xiaoling Tang ◽  
Jianchao Zhang ◽  
Ying Cai ◽  
Shiying Miao ◽  
Shudong Zong ◽  
...  
Keyword(s):  
Membrane Protein ◽  
Sperm Membrane

scholarly journals Caenorhabditis elegans sperm membrane protein interactome

2018 ◽  
Vol 98 (6) ◽  
pp. 776-783 ◽  
Author(s):  
Matthew R Marcello ◽  
Marina Druzhinina ◽  
Andrew Singson
Keyword(s):  
Caenorhabditis Elegans ◽  
Membrane Protein ◽  
Protein Interactome ◽  
Sperm Membrane

scholarly journals Mutation of a putative sperm membrane protein in Caenorhabditis elegans prevents sperm differentiation but not its associated meiotic divisions.

1992 ◽  
Vol 119 (1) ◽  
pp. 55-68 ◽  
Author(s):  
S W L'Hernault ◽  
P M Arduengo
Keyword(s):  
Caenorhabditis Elegans ◽  
Membrane Protein ◽  
Molecular Basis ◽  
Close Association ◽  
Integral Membrane Protein ◽  
Nematode Caenorhabditis Elegans ◽  
C Elegans ◽  
Fibrous Body ◽  
Sperm Membrane ◽  
Internal Membrane Structure

Spermatogenesis in the nematode Caenorhabditis elegans uses unusual organelles, called the fibrous body-membranous organelle (FB-MO) complexes, to prepackage and deliver macromolecules to spermatids during cytokinesis that accompanies the second meiotic division. Mutations in the spe-4 (spermatogenesis-defective) gene disrupt these organelles and prevent cytokinesis during spermatogenesis, but do not prevent completion of the meiotic nuclear divisions that normally accompany spermatid formation. We report an ultrastructural analysis of spe-4 mutant sperm where the normally close association of the FB's with the MO's and the double layered membrane surrounding the FB's are both defective. The internal membrane structure of the MO's is also disrupted in spe-4 mutant sperm. Although sperm morphogenesis in spe-4 mutants arrests prior to the formation of spermatids, meiosis can apparently be completed so that haploid nuclei reside in an arrested spermatocyte. We have cloned the spe-4 gene in order to understand its role during spermatogenesis and the molecular basis of how mutation of this gene disrupts this process. The spe-4 gene encodes an approximately 1.5-kb mRNA that is expressed during spermatogenesis, and the sequence of this gene suggests that it encodes an integral membrane protein. These data suggest that mutation of an integral membrane protein within FB-MO complexes disrupts morphogenesis and prevents formation of spermatids but does not affect completion of the meiotic nuclear divisions in C. elegans sperm.

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