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Lee, Syng-Ill,Yu, Yun-Jung,Turner, R. James The Official Publication of Korean Academy of Oral 1994 International Journal of Oral Biology Vol.18 No.2
In rat parotid basolateral membranes the presence of a 160 kD protein can be labeled with the irreversible sulfhydryl reagent [^14C]-N-ethyl maleimide in a bumetanide-protectable fasion. The previous results suggest that the existence of an esential sulfhydryl group is closely associated with the bumetanide-binding site on the parotid Na/K/Cl cotransporter, provide strong evidence that this protein is a part or all of the parotid bumetanide-binding site. When this protein is treated with endoglycosidase F/N-glycosidase F to remove N-linked oligosaccharides, its apparent molecular weight decreases to 135 kD. The bumetanide-binding protein was purified using two preparative electrophoresis steps. First, a Triton X-100 extract enriched in this protein was run on preparative electophoresis to obtain fractions containing proteins in the 160 kD range. These were then deglycosylated with endoglycosidase F/N-glycosidase F and selected fractions were pooled and rerun on preparative electrophoresis to obtain a final 135 kD fraction. The enrichment of the bumetanide-binding protein on this final 135kD fraction estimated from [^14C]-N-ethylmaleimide labeling was approximately 48 times relative to the starting membrane extract. Since the bumetanide-binding site represents approximately 2% of the total protein this starting extract, this enrichment indicates a high degree of purity of this protein in the 135 kD fraction.