Isolation and characterization of a sulfated glycoprotein from rabbit small intestine

Complex saccharides were extracted with 0.9% NaCl at 0°C from rabbit small intestine, then fractionated with cetylpyridinium chloride (CPC), followed by DEAE-Sephadex A-25 column chromatography and by GEON-zone electrophoresis. An acidic glycoprotein (Fr. A-l) thus obtained was shown to be homogeneo...

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Published inJournal of biochemistry (Tokyo) Vol. 84; no. 6; pp. 1587 - 1592
Main Authors MUNAKATA, Hiroshi, YOSIZAWA, Zensaku
Format Journal Article
LanguageEnglish
Published England Oxford University Press 01.01.1978
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Summary:Complex saccharides were extracted with 0.9% NaCl at 0°C from rabbit small intestine, then fractionated with cetylpyridinium chloride (CPC), followed by DEAE-Sephadex A-25 column chromatography and by GEON-zone electrophoresis. An acidic glycoprotein (Fr. A-l) thus obtained was shown to be homogeneous by electrophoreses on cellulose acetate membrane and on sodium dodecyl sulfate (SDS)-polyacrylamide gel, as well as by gel filtration on Sepharose 4B. It contained 40.0% protein, 52.7% carbohydrate, and 1.6% sulfate. The principal sugars in the sulfated glycoprotein were galactose, glucosamine, galactosamine, and siahc acid. Small quantities of mannose, L-fucose, and glucose were also present. Glutamic acid, threonine, aspartic acid, alanine, serine, leucine, proline, glycine, valine, and histidine were the major amino acids of the protein moiety. Small amounts of other basic amino acids, sulfur-containing amino acids and aromatic amino acids were also present.
Bibliography:L
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ArticleID:84.6.1587
1This work was supported by a grant from the Ministry of Education, Science and Culture of Japan
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content type line 23
ISSN:0021-924X
1756-2651
DOI:10.1093/oxfordjournals.jbchem.a132284