Isolation of a novel lectin from the hemolymph of horseshoe crabs Limulus polyphemus and its hemagglutinating properties

Autor:	Toshio Yamakawa, Isami Tsuboi, Hajime Kubota, Masahito Matsukawa, Kohmei Yanagi
Rok vydání:	1996
Předmět:	chemistry.chemical_classification Chromatography biology Molecular mass Physiology Lectin biology.organism_classification Biochemistry Hexosamines Horseshoe crab Affinity chromatography chemistry Limulus Hemolymph biology.protein Glycophorin Molecular Biology
Zdroj:	Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology. 113:137-142
ISSN:	1096-4959
DOI:	10.1016/0305-0491(96)02009-3
Popis:	A novel lectin was isolated from hemolymph of American horseshoe crab Limulus polyphemus by using human glycophorin A N affinity chromatography and Sephacryl S-300 gel filtration. The lectin's molecular weight was approximately 1700 kDa; being composed of 24 identical subunits with molecular weights of 70 kDa. The hemagglutinating activity of the lectin against human erythrocytes was strongly inhibited by human glycophorin A N and weakly inhibited by N -acetylhexosamines, although not inhibited by neutral sugars, or hexosamines. This lectin required no Ca 2+ for hemagglutinating human, rabbit and equine erythrocytes, respectively.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_________::fe4e55474c71ac43b777b967b7079226 https://doi.org/10.1016/0305-0491(96)02009-3 Zobrazit plný text záznamu Full Text from ScienceDirect