Studies on human cervical mucus: The effect of proteases on cervical mucus glycoproteins functions

The influence of proteolytic enzymes on human cervical mucus glycoproteins has been investigated to assess their influence on cervical function, sperm migration and penetration. The main component of estrogenic cervical mucus, a high molecular weight glycoprotein was treated with Pronase, trypsin and chymotrypsin, and the enzyme-resistant glycoprotein was purified by gel filtration on Bio-Gel P-200 and Sepharose 2-B. A macromolecular component in good yield was recovered containing carbohydrate and protein moieties. Asialoglycoprotein on treatment with Pronase, trypsin and chymotrypsin released more than one glycoproteins. The carbohydrate and amino acid composition of the native and degraded glycoproteins were similar in composition with changes in molecular proportions. Sequential glycosidases treatment lectin binding and Smith's degradation established main structural features of degraded glycoproteins that showed some differences to that of native glycoprotein. The influence of proteinases on cervical mucus glycoproteins and a possible mechanism of sperm penetration through the cervical mucus and enzyme treated glycoproteins is investigated. It has been shown that in midcycle human and simian cervical mucus glycoproteins there are common epitopes.