Abstract
A glycoprotein of an apparent molecular weight of 250,000 has been purified from human amniotic fluid. Its amino acid composition includes trace amounts of hydroxyproline but no hydroxylysine. It has relatively high contents of aspartic acid, glutamic acid, glycine and leucine. It contains approximately 6% hexose, 2% sialic acid, and 4% glucosamine. The hexoses are galactose, mannose and fucose. No glucose and galactosamine can be detected. This high-molecular-weight glycoprotein cross-reacts with an antiserum prepared in rabbits against a glycoprotein of similar size and composition isolated from the alveolar secretions of humans suffering from pulmonary alveolar proteinosis [20]. It therefore appears that the glycoprotein isolated from human amniotic fluid is similar in size, composition and immunological properties to the glycoprotein present in human alveolar secretions.
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