Abstract:
:Tyrosine kinase was extracted from rat spleen. Some 60% of the activity with angiotensin as the substrate was found in the cytoplasmic supernatant obtained at 100,000g. Two kinases in the supernatant, TKI and -II were purified 170- and 600-fold, respectively, by column chromatography. The molecular weights of TKI and -II were estimated to be 38,000 and 30,000 by Sephacryl S-200 gel filtration, and to be 42,000 and 36,000 by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Experiments with various protease inhibitors suggested that these kinases were not the artifacts of proteolysis. Both kinases autophosphorylated their tyrosine residues. They had different Kms for angiotensin II, and for ATP, but similar dependencies on temperature and on divalent metal ions.
journal_name
Arch Biochem Biophysjournal_title
Archives of biochemistry and biophysicsauthors
Hasuma T,Inoue A,Higashi Y,Morisawa S,Yukioka Mdoi
10.1016/0003-9861(90)90537-9subject
Has Abstractpub_date
1990-07-01 00:00:00pages
206-10issue
1eissn
0003-9861issn
1096-0384pii
0003-9861(90)90537-9journal_volume
280pub_type
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journal_title:Archives of biochemistry and biophysics
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更新日期:2004-05-15 00:00:00
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pub_type: 杂志文章
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