Abstract
Abstract The molecular structure of a sulfated glycoprotein from chick chorioallantoic fluid has been investigated. The effect of alkali and alkali-borohydride under various conditions has been shown to lead to quantitatively and qualitatively different products of elimination and reduction. The carbohydrate chains of the products, by gel filtration, were heterogeneous, ranging from an average molecular weight of 1,100 to 2,600. The purified glycoprotein (mol wt 26,000 by gel filtration) contained a series of fatty acids bound to carbohydrate in ester linkage. The sialic acid of the glycoprotein was characterized as N-acetylneuraminic acid.
Highlights
MethodsPreparation oj Glycoprotein from Chick Allantoic Fluid Injected with ZnJluenza Virus (Japan 170/6ZA2)-The method was essentially similar to those used in this laboratory for isolation of keratan sulfate (6)
The molecular structure of a sulfated glycoprotein from chick chorioallantoic fluid has been investigated
It has been shown that the host factor of influenza virus grown in chick embryos is an integral part of the viral particle
Summary
Preparation oj Glycoprotein from Chick Allantoic Fluid Injected with ZnJluenza Virus (Japan 170/6ZA2)-The method was essentially similar to those used in this laboratory for isolation of keratan sulfate (6). The product was further purified by gel filtration on a Rio-Gel l-‘-100 column (2.50 X 230 cm) with 0.5 N NaCl as eluent (yield 1.38 mg per g of acetone powder). In another preparation, the CAFS was digested further with pronase for 3 days with no apparent change in the size of the molecule and amino acid composition. The products were homogeneous in ion exchange chromatography on a DEAE-Sephadex column in pH 6.2 acetate buffer with a linear gradient of 0.3 M to 1.5 M NaCl, electrophoresis on Sepraphore at pH 5.0 and 1.8, and gel filtration chromatography on a Sephadex column (1.04 x 90 cm) with 0.025 N NaCl solution as eluent, as well as on a Rio-Gel I’-200 column
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