S. Capellacci et al., One step purification of glucose-6-phosphate dehydrogenase from brain areas by immunoaffinity chromatography, BIOTECH LET, 23(5), 2001, pp. 353-357
Glucose-6-phosphate dehydrogenase was purified from rabbit brain cortex usi
ng a single immunoaffinity chromatographic step and was contaminated only b
y a 50 kDa protein. The proteins, separated by SDS-PAGE, were sequenced: th
e glucose-6-phosphate dehydrogenase was blocked at the N-terminal, the co-e
luted protein was similar to alpha -tubulin. Our technique can be applied t
o purification and sequencing of the enzyme from brain areas or to measure
its turnover rate in cultured cells.