Some preliminary observations on the liquefaction of human semen.
Liquefaction of human semen in vitro was studied by scanning electron microscopy, determinations of total protein, free amino acid and phosphate and by correlation analysis. During liquefaction of the coagulum, its fibers were transformed into globular bodies that fused to form the homogeneous liquefied semen. It was found that the parts of the ejaculate taking more time to liquefy possessed higher concentration of protein than those of the parts liquefied earlier, a relation also appeared to exist with the whole ejaculates. Release rate of phosphate during macroscopic lysis and free reducing sugar level of ejaculates demonstrated significant negative correlations with liquefaction time which could be shortened using reductants.
D000328:Adult; D000596:Amino Acids / Q000032:analysis; D006801:Humans; D008297:Male; D008855:Microscopy, Electron, Scanning; D008875:Middle Aged; D010710:Phosphates / Q000032:analysis; D011506:Proteins / Q000032:analysis; D012661:Semen; D012995:Solubility; D013073:Sperm Agglutination; D013997:Time Factors
D000596:Amino Acids; D010710:Phosphates; D011506:Proteins