Purification and immunochemical characterization of human adrenal tyrosine hydroxylase |
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| Authors: | Kohichi Kojima Makio Mogi Kazuhiro Oka Toshiharu Nagatsu |
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| Affiliation: | 1. Laboratory of Cell Physiology, Department of Life Chemistry, Graduate School at Nagatsuta, Tokyo, Japan;2. Institute of Technology, Yokohama 227, Japan |
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| Abstract: | Tyrosine hydroxylase (TH) was purified from the soluble fraction of human adrenal glands. The enzyme in human adrenal glands that was purified to apparent homogeneity had an apparent Mr of about 280,000. Sodium dodecyl sulfate (SDS) gel electrophoresis gave a single band with a Mr of 60,000 similar to the Mr of bovine adrenal enzyme. The enzyme is considered to be composed of four identical subunits. The specific activity of the final preparation was approximately 310 nmol 3,4-dihydroxyphenylalanine (DOPA) formed/min/mg protein. The use of the “Western Blot” method showed that human adrenal TH did not aggregate as rapidly as bovine adrenal TH. |
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| Keywords: | TH tyrosine hydroxylase SDS sodium dodecyl sulfate DOPA 3,4-dihydroxyphenylalanine PAGE polyacrylamide gel electrophoresis PBS phosphate-buffered saline BSA bovine serum albumin |
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