1997
DOI: 10.1016/s0736-5748(96)00077-9
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Novel 29 kDa heparin‐binding lectin from human foetal brain

Abstract: Heparin inhibitable lectins are physiologically important because of their interactions with extracellular matrix and with other cell surface glycoconjugates. However, due to the unstable nature of these animal lectins, it becomes necessary to purify them in the shortest possible time. In the present study, a chromatographic procedure was developed to separate heparin inhibitable lectin activity. Lectin activities from human foetal brain were separated on a Q-Sepharose column employing different equilibration … Show more

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Cited by 2 publications
(1 citation statement)
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“…The hyaluronectin expression is developmentally different from that of its ligand hyaluronic acid [Marret et al, 1994], in such a way that a direct interaction of the one with the other is puzzling. Another heparin-inhibitable lectin was isolated from human fetal brain with a M r of 29 kDa showing an optimal pH of around 7.0 and stimulated by Mn 2+ ions [Basu et al, 1997]. In different fetal brain regions gave the highest content in the cerebral cortex in the fetal cerebral cortex gave the highest value with a mitochondrial fraction.…”
Section: Glycosaminoglycan Binding Lectinsmentioning
confidence: 99%
“…The hyaluronectin expression is developmentally different from that of its ligand hyaluronic acid [Marret et al, 1994], in such a way that a direct interaction of the one with the other is puzzling. Another heparin-inhibitable lectin was isolated from human fetal brain with a M r of 29 kDa showing an optimal pH of around 7.0 and stimulated by Mn 2+ ions [Basu et al, 1997]. In different fetal brain regions gave the highest content in the cerebral cortex in the fetal cerebral cortex gave the highest value with a mitochondrial fraction.…”
Section: Glycosaminoglycan Binding Lectinsmentioning
confidence: 99%