ISOELECTRIC FORMS OF CLUSTERIN ISOLATED FROM RAM RETE TESTIS FLUID AND FROM SECRETIONS OF PRIMARY CULTURES OF RAM AND RAT SERTOLI-CELL-ENRICHED PREPARATIONS

Clusterin, a cell aggregating factor isolated from ram rete testis fluid (RTF), contained 14.7% hexoses,13.6% glucosamine, and 7.9% sialic acid. The isoelectric point (pI) of the predominant electrophoretic form of clusterin from ram RTF is 3.7. After treatment with neuraminidase, the pI values become more basic, with the majority of the material being eluted from a chromatofocusing column at pH value between 4.9 and 5.1. Intact clusterin binds quantitatively to wheat germ agglutinin-Sepharose 6 MB, but after treatment with neuraminidase only 49% specifically binds. Clusterin isolated from proteins secreted by primary cultures of ram Sertoli-cell-enriched preparations had properties similar to those of intact clusterin isolated from ram RTF. In contrast, clusterin isolated from proteins secreted by primary cultures of rat Sertoli- or granulosa-cell-enriched preparations has isoelectric forms which more closely resemble those of neuraminidase-treated ram clusterin.