Isolation and characterization of a mannan-binding protein associated with the early chick embryo

To study the role of the mannan-binding activity in embryonic development it is necessary to purify and characterize the lectin, which has proved difficult; however, the authors have been able to effect a 27-fold purification using hydroxyapatite in a batch procedure, this method and some of the pro...

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Bibliographic Details
Published in:FEBS letters 1981-12, Vol.136 (1), p.105-110
Main Authors: Rutherford, Nicholas G., Cook, Geoffrey M.W.
Format: Article
Language:English
Subjects:
Animals
Carrier Proteins - antagonists & inhibitors
Carrier Proteins - isolation & purification
Carrier Proteins - metabolism
Chick Embryo - analysis
chick embryos
Chromatography, Affinity
Chromatography, Gel
Collectins
Electrophoresis, Polyacrylamide Gel
Female
Glycoproteins - pharmacology
Hemagglutinins - metabolism
mannan-binding protein
Mannans - pharmacology
purification
Structure-Activity Relationship
Vitelline Membrane - analysis
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Summary:To study the role of the mannan-binding activity in embryonic development it is necessary to purify and characterize the lectin, which has proved difficult; however, the authors have been able to effect a 27-fold purification using hydroxyapatite in a batch procedure, this method and some of the properties of the resulting meterial are described.
ISSN:0014-5793
1873-3468
DOI:10.1016/0014-5793(81)81224-0