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Soluble heparin-binding lectins from human brain: purification, specificity and relationship to an heparin-binding growth factor.

作者信息

Eloumami H, Bladier D, Caruelle D, Courty J, Joubert R, Caron M

机构信息

Laboratoire de Biochimie et Technologie des Protéines, Université Paris-Nord, Bobigny, France.

出版信息

Int J Biochem. 1990;22(5):539-44. doi: 10.1016/0020-711x(90)90270-d.

DOI:10.1016/0020-711x(90)90270-d
PMID:1693345
Abstract
  1. An heparin-binding lectin activity was detected in soluble extracts of human brain. Three polypeptide chains were purified by affinity chromatography on heparin-Sepharose. Their Mrs estimated by polyacrylamide gel electrophoresis were 13,000, 14,500 and 16,000. 2. Several glycosaminoglycans were potent inhibitors of their hemagglutination activity. 3. From the pool of purified lectins three peaks were separated by reversed-phase high-performance liquid chromatography. They were indistinguishable by activity criteria (hemagglutination, stimulation of endothelial cell growth), and immunological relationship was found between one of them and acidic fibroblast growth factor (aFGF).
摘要

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