Diversity of glutamate dehydrogenase in human brain.
作者： Gulnur Sh Burbaeva , Marina S Turishcheva , Elena A Vorobyeva , Olga K Savushkina , Elena B Tereshkina
DOI: 10.1016/S0278-5846(01)00273-1
关键词:
摘要: Three forms of glutamate dehydrogenase (GDH, EC 1.4.1.3) are purified from human brain tissue. Two them, named GDH I (consisting 58+/-1-kDa subunit) and II 56+/-1 -kDa subunit), readily solubilized the third one, III 56+/-1-kDa is a membrane-associated (particulate bound) isoform. Kinetic constants were determined for III. These found to differ in hydrophobicity as indicated by different affinity Phenyl-Sepharose. All three showed microheterogeneity on two-dimensional (2-D) gel electrophoresis. Specific polyclonal antibodies, which enable determine levels immunoreactivities all extracts enzyme-chemiluminescent amplified (ECL)-Western immunoblotting, obtained.
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