One step purification of glucose-6-phosphate dehydrogenase from brain areas by immunoaffinity chromatography View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2001-03

AUTHORS

Samuela Capellacci, Gianfranca Aluigi, Laura Tabellini, Paolino Ninfali

ABSTRACT

Glucose-6-phosphate dehydrogenase was purified from rabbit brain cortex using a single immunoaffinity chromatographic step and was contaminated only by a 50 kDa protein. The proteins, separated by SDS-PAGE, were sequenced: the glucose-6-phosphate dehydrogenase was blocked at the N-terminal, the co-eluted protein was similar to α-tubulin. Our technique can be applied to purification and sequencing of the enzyme from brain areas or to measure its turnover rate in cultured cells. More... »

PAGES

353-357

Identifiers

URI

http://scigraph.springernature.com/pub.10.1023/a:1005645321854

DOI

http://dx.doi.org/10.1023/a:1005645321854

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1043747673


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