Literature DB >> 227467

Properties of rat liver nuclear protein kinases.

W Thornburg, S Gamo, A F O'Malley, T J Lindell.   

Abstract

Two cyclic nucleotide-independent protein kinases (ATP:protein phosphotransferase, EC 2.7.1.37) have been purified to homogeneity from rat liver nuclei. While these enzymes have many similar catalytic properties (preference for acid rather than basic proteins), they differ in molecular weight and subunit composition. Protein kinase NII will utilize ATP and GTP as phosphate donors while protein kinase NI will only effectively use ATP. Both enzymes reveal an unusual activation by Fe2+.

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Year:  1979        PMID: 227467     DOI: 10.1016/0005-2744(79)90222-5

Source DB:  PubMed          Journal:  Biochim Biophys Acta        ISSN: 0006-3002


  5 in total

1.  Binding of a pea nuclear protein to promoters of certain photoregulated genes is modulated by phosphorylation.

Authors:  N Datta; A R Cashmore
Journal:  Plant Cell       Date:  1989-11       Impact factor: 11.277

2.  Studies on protein kinases involved in regulation of nucleocytoplasmic mRNA transport.

Authors:  H C Schröder; M Rottmann; R Wenger; M Bachmann; A Dorn; W E Müller
Journal:  Biochem J       Date:  1988-06-15       Impact factor: 3.857

3.  Characteristics of polyamine stimulation of cyclic nucleotide-independent protein kinase reactions.

Authors:  K Ahmed; S A Goueli; H G Williams-Ashman
Journal:  Biochem J       Date:  1985-12-15       Impact factor: 3.857

4.  Polyamine-stimulated phosphorylation of prostatic spermine-binding protein is mediated only by cyclic AMP-independent protein kinases.

Authors:  S A Goueli; A T Davis; R A Hiipakka; S Liao; K Ahmed
Journal:  Biochem J       Date:  1985-09-01       Impact factor: 3.857

5.  Casein kinase II is a predominantly nuclear enzyme.

Authors:  W Krek; G Maridor; E A Nigg
Journal:  J Cell Biol       Date:  1992-01       Impact factor: 10.539

  5 in total

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