Characterization of Sperm Agglutinating Factor Isolated from Staphylococcus Aureus and its Corresponding Receptor from Spermatozoa
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چکیده
Spermagglutination factor isolated from Staphylococcus aureus showed spermagglutinating and spermicidal properties in vitro. In an attempt to characterize SAF, it was tested for the various factors produced by S. aureus viz. catalase, coagulase, hemolysins, protease, lipase, phospholipase C, nuclease and protein A. As, SAF did not show any of these activities, therefore to identify it, peptide mass fingerprinting using Matrix Assisted Laser Desorption Ionization-Time of flight (MALDI-TOF) was done. Matching of the mass spectrum in NCBI database showed sequence homology with hypothetical protein BACPEC_00178 of Bacteroides pectinophilus ATCC 43243. SAF conjugated with FITC was able to bind to spermatozoa indicating the presence of receptor on sperm surface. Calorimetric analysis of SAF and this purified receptor interaction showed the binding constant, enthalpy of binding ΔH° as 1130/M and -11.6kJ/mole while the values of free energy and entropy were -18.1kJ/mole and 20.9J/moleK, respectively. The receptor showed sequence similarities with chain A crystal structure of Ga module complexed with human serum albumin when subjected to MALDI-TOF. 62 S. Kaur and V. Prabha
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