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Previously, we identified 260\/280\u2009kDa oligomers (termed eFGL\u2014Epididymal Fibrinogen\u2010Like oligomer) are composed of two disulfide\u2010linked subunits: a 64\u2009kDa polypeptide identified as fibrinogen\u2010like protein\u20102 (FGL2) and a 33\u2009kDa polypeptide identified as fibrinogen\u2010like protein\u20101 (FGL1). Our morphological studies demonstrated that the eFGL, secreted from the principal cells of the cauda epididymis, is polymerized into a death cocoon\u2010like complex (DCF), masking defective luminal spermatozoa but, not the viable sperm population. In the present study, we purified FGL2 from hamster cauda epididymal fluid toward\u00a0homogeneity and its prothrombinase catalytic activity was examined. Time\u2010course conversion studies revealed that all prothrombin was converted to thrombin by purified hamster FGL2. Our biochemical studies demonstrate that FGL2 is a lipid\u2010activated serine protease and functions as a lectin by binding specific carbohydrate residues. Co\u2010immunoprecipitation analysis demonstrated that FGL2 of cauda epididymal fluid is ubiquitinated but not the FGL1. We propose that FGL2\/FGL1 oligomers represent a novel and unique mechanism to shield the viable sperm population from degenerating spermatozoa contained within the tubule lumen.<\/jats:p>","DOI":"10.1002\/mrd.23438","type":"journal-article","created":{"date-parts":[[2020,11,20]],"date-time":"2020-11-20T23:00:54Z","timestamp":1605913254000},"page":"1206-1218","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":2,"title":["Fibrinogen\u2010related protein, FGL2, of hamster cauda epididymal fluid: Purification, kinetic analysis of its prothrombinase activity, and its role in segregation of nonviable spermatozoa"],"prefix":"10.1002","volume":"87","author":[{"given":"Subir K.","family":"Nagdas","sequence":"first","affiliation":[{"name":"Department of Chemistry,\u00a0Physics &amp; Materials Science Fayetteville State University  Fayetteville North Carolina USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Shamar","family":"Wallace","sequence":"additional","affiliation":[{"name":"Department of Chemistry,\u00a0Physics &amp; Materials Science Fayetteville State University  Fayetteville North Carolina USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Don","family":"Eaford","sequence":"additional","affiliation":[{"name":"Department of Chemistry,\u00a0Physics &amp; Materials Science Fayetteville State University  Fayetteville North Carolina USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Rashad","family":"Baker","sequence":"additional","affiliation":[{"name":"Department of Chemistry,\u00a0Physics &amp; Materials Science Fayetteville State University  Fayetteville North Carolina USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Ky'ara","family":"Carr","sequence":"additional","affiliation":[{"name":"Department of Chemistry,\u00a0Physics &amp; Materials Science Fayetteville State University  Fayetteville North Carolina USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Samir S.","family":"Raychoudhuri","sequence":"additional","affiliation":[{"name":"Department of Biology,\u00a0Chemistry and Environmental Health Science Benedict College  Columbia South Carolina USA"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"311","published-online":{"date-parts":[[2020,11,20]]},"reference":[{"key":"e_1_2_5_2_1","doi-asserted-by":"publisher","DOI":"10.1016\/S0303-7207(99)00060-X"},{"key":"e_1_2_5_3_1","first-page":"587","article-title":"Apoptosis in human ejaculated sperm cells (Notulae seminologicae 9)","volume":"28","author":"Baccetti B. 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