A glycoprotein was isolated from the bovine gallbladder secretion. The glycoprotein was purified on Bio-Gel P-200 and by subsequent mild treatment with Pronase. The Pronase treated glycoprotein was further purified by gel chromarography on Sepharose 4B and by ion-exchange chromatography. The purified glycoprotein was subjected to alkaline degradation-borohydride reduction. The liberated oligosaccharide alditols were purified by gel filtration, and separated into neutral and acidic oligosaccharides. Four neutral oligosaccharides, after purification, were characterized by chemical and enzymatic studies and were assigned the following structures and partial structure.
F SMITH ,J T LAMOUNT ,N UDDIN ,S A HUSSAIN ,BER NARD ,S M AJZA ,
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