Open Access. Powered by Scholars. Published by Universities.®
Articles 1 - 1 of 1
Full-Text Articles in Life Sciences
Nerve Tissue-Specific Human Glutamate Dehydrogenase That Is Thermolabile And Highly Regulated By Adp / P. Shashidharan, Donald D. Clarke, Naveed Ahmed, Nicholas Moschonas, And Andreas Plaitakis Department Of Neurology, Mount Sinai School Of Medicine, New York; Department Of Chemistry, Fordham University, Bronx New York, Usa; And Department Of Biology And School Of Health Sciences, University Of Crete, Crete, Greece, P. Shashidharan, Donald Dudley Clarke Phd, Naveed Ahmed, Nicholas Moschonas
Nerve Tissue-Specific Human Glutamate Dehydrogenase That Is Thermolabile And Highly Regulated By Adp / P. Shashidharan, Donald D. Clarke, Naveed Ahmed, Nicholas Moschonas, And Andreas Plaitakis Department Of Neurology, Mount Sinai School Of Medicine, New York; Department Of Chemistry, Fordham University, Bronx New York, Usa; And Department Of Biology And School Of Health Sciences, University Of Crete, Crete, Greece, P. Shashidharan, Donald Dudley Clarke Phd, Naveed Ahmed, Nicholas Moschonas
Chemistry Faculty Publications
Glutamate dehydrogenase (GDH), an enzyme that is central to the metabolism of glutamate, is present at high levels in the mammalian brain. Studies on human leukocytes and rat brain suggested the presence of two GDH activities differing in thermal stability and allosteric regulation, but molecular biological investigations led to the cloning of two human GDH-specific genes encoding highly homologous polypeptides. The first gene, designated GLUD1, is expressed in all tissues (housekeeping GDH), whereas the second gene, designated GLUD2, is expressed specifically in neural and testicular tissues. In this study, we obtained both GDH isoenzymes in pure form by expressing a …