Michael A. Tranulis, Berit Christophersen, Borgar Borrebaek
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引用次数: 10
Abstract
The monomer molecular mass of glucose dehydrogenase (GDH, EC 1.1.1.47) from rainbow trout liver and beef liver were estimated to be 90 kDa for both enzymes, by electrophoresis in the presence of Na-dodecyl-SO4 (SDS). The 90-kDa proteins were partially degraded to about 60 kDa when purified with a delayed procedure without protease inhibitors. Tryptic cleavage of the 90-kDa proteins gave fragments of about 60 kDa and 30 kDa, being similar for trout and beef GDH. Isoelectric points, kinetic and thermodynamic properties of the two enzymes are markedly different. Triton X-100 stimulated and stabilized the reactions catalysed by the purified enzymes.
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