Abstract:
:A phosphoprotein with associated tyrosine kinase activity has been purified from a 26,000 x g particulate fraction of rat spleen. The molecular weight of the native kinase is 85-90 kDa as estimated by gel permeation chromatography on Superdex 200 while SDS/PAGE of an autophosphorylated sample indicated a single 28-kDa band in which the radiolabel was alkali-stable. The SDS/PAGE following the incubation with 5'-p-fluorosulfonylbenzoyl[8-14C]adenosine reveals a single labeled band migrating at a molecular weight of approximately 28 kDa. The enzyme shows very restricted substrate specificity. Casein and, to a lesser degree, the random polypeptide poly(Tyr1,Glu4) were phosphorylated. The enzyme exhibits a preference for Mn2+ over Mg2+ as an activator.
journal_name
Biochem Biophys Res Communjournal_title
Biochemical and biophysical research communicationsauthors
Borowski P,Medem S,Laufs Rdoi
10.1006/bbrc.1993.1877subject
Has Abstractpub_date
1993-07-30 00:00:00pages
691-7issue
2eissn
0006-291Xissn
1090-2104pii
S0006-291X(83)71877-2journal_volume
194pub_type
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