Premium
Lactose‐ and Heparin‐Inhibitable Agglutinin from Human Fetal Brain
Author(s) -
Mandal S.,
Mahajan R. G.
Publication year - 1990
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/j.1471-4159.1990.tb13313.x
Subject(s) - agglutinin , affinity chromatography , biochemistry , lactose , lectin , gel electrophoresis , sepharose , soybean agglutinin , chemistry , size exclusion chromatography , microbiology and biotechnology , chromatography , biology , enzyme
An agglutinin activity which was sensitive to lactose and heparin was estimated during prenatal brain development. The agglutinin showed higher specific activities in cerebral cortex and midbrain. There was an increase in lectin specific activity in all the brain regions with development. In addition to brain, other fetal organs also showed the presence of developmentally regulated agglutinin. Cerebral cortical agglutinin was purified by Sepharose CL‐6B gel filtration and asialofetuin‐ and heparin‐Sepharose affinity chromatography. Purified agglutinin was strongly inhibited by lactose, asialofetuin, and heparin. It showed no requirement for divalent cations and was maximally active at pH 8.0. Electrophoretic characterization showed the aggregate nature of the agglutinin, and sodium dodecyl sulfate‐polyacrylamide gel electrophoresis gave subunit molecular weights of 58,000, 45,000, and 24,000.