Two splenic soluble tyrosine kinases from the rat.
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.
Hasuma
T
T
Department of Biochemistry, Osaka City University Medical School, Japan.
Inoue
A
A
Higashi
Y
Y
Morisawa
S
S
Yukioka
M
M
D000818:Animals; D002413:Cations, Divalent; D002467:Cell Nucleus / Q000201:enzymology; D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D003600:Cytosol / Q000201:enzymology; D007527:Isoenzymes / Q000302:isolation & purification / Q000378:metabolism*; D007700:Kinetics; D008970:Molecular Weight; D011505:Protein-Tyrosine Kinases / Q000302:isolation & purification / Q000378:metabolism*; D051381:Rats; D013154:Spleen / Q000201:enzymology*; D013347:Subcellular Fractions / Q000201:enzymology; D013816:Thermodynamics
D002413:Cations, Divalent; D007527:Isoenzymes; D011505:Protein-Tyrosine Kinases