scholarly journals Reproductive biotechnology in animal husbandry - current status and future prospects

2015 ◽  
Vol 31 (4) ◽  
pp. 467-480 ◽  
Author(s):  
M. Ivanova ◽  
D. Gradinarska ◽  
D. Daskalova
Keyword(s):  
Seminal Plasma ◽  
Plasma Proteins ◽  
Polyacrylamide Gel Electrophoresis ◽  
Animal Husbandry ◽  
Biological Evaluation ◽  
Size Exclusion ◽  
Current Status ◽  
Computer Assisted ◽  
Biological Potential ◽  
Seminal Plasma Proteins

To date there is still no optimal biotechnology which ensures maximum preservation of the functional parameters of the spermatozoa from buffaloes, boars and dogs. The aim of this research is to study the biological potential of seminal plasma proteins that are specific only to ejaculates with high cryotolerance and good quality parameters of the spermatozoa. The motility and velocity parameters of the spermatozoa were assessed by computer-assisted sperm analysis. Seminal plasma proteins were separated by size-exclusion liquid chromatography and characterized by polyacrylamide gel electrophoresis and mass spectrometry. Based on the results obtained, sperm diluents and methods for biological evaluation of the fertilization potential of the spermatozoa from buffalo bulls, boars and dogs were created and proposed for practical application.

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

Aggregated Forms of Bull Seminal Plasma Proteins and Their Heparin-Binding Activity

2004 ◽  
Vol 69 (3) ◽  
pp. 616-630 ◽  
Author(s):  
Petra Jelínková ◽  
Helena Ryšlavá ◽  
Jiří Liberda ◽  
Věra Jonáková ◽  
Marie Tichá
Keyword(s):  
Molecular Weight ◽  
Seminal Plasma ◽  
Plasma Proteins ◽  
Sodium Dodecyl ◽  
Reversed Phase ◽  
Binding Activity ◽  
Size Exclusion ◽  
Heparin Binding ◽  
Aggregation State ◽  
Seminal Plasma Proteins

Heparin-binding activity of bull seminal plasma proteins was shown to be dependent on their aggregation state. The protein fraction interacting with immobilized heparin was characterized by large polydispersity in the region of molecular weight of 60 000-10 000, while that not retained on the affinity carrier was present as aggregates with molecular weight >100 000. Components of heparin-binding and non-heparin-binding fractions were separated by RP HPLC (reversed-phase HPLC) and analyzed by SDS (sodium dodecyl sulfate) electrophoresis and N-terminal sequencing. Size exclusion chromatography of whole seminal plasma and heparin-binding proteins in the presence of D-fructose (as a component of seminal plasma) showed that the region of molecular weights of protein-associated forms was shifted to lower values. An increase of heparin-binding activity of bull proteins, as determined by ELBA (Enzyme-Linked Binding Assay), correlates with a decrease of their aggregation state. The modulation of the aggregation state of bull proteins by seminal plasma components and, in this way, also of their heparin-binding properties suggests possible mechanisms for capacitation mediated by these proteins.

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