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1986 (2)
1981 (1)
1976 (1)
1Author    Ruth Hracky, Jürgen SollRequires cookie*
 Title    Protein Phosphorylation — Dephosphorylation in the Cytosol of Pea Mesophyll Cells  
 Abstract    Soluble protein kinase and protein phosphatase activities were localized in the cytosol of pea mesophyll cells using protoplasts fractionation techniques. The molecular weights of the phos-phorylated cytosolic proteins, as determined by polyacrylamide gel electrophoresis, were 68, 55, 46, 38, 36, 30, 22 and 12 kDa. Histone and, to a much lesser extent, casein but not phosvitin were accepted as exogenous substrates. In every case serine served as acceptor amino acid for the phosphate residue. The protein phosphorylation activity had an alkaline pH optimum, and showed no response to varying Mg2+, Ca2+, Pn cyclo-AMP or calmodulin concentrations. The kinase activity was competitively inhibited by ADP and pyrophosphate with apparent K t values of 0.5 and 0.17 m M , respectively. High ATP concentrations (1 -4 m M) resulted in a strong decrease of radioactivity in the ,2P labeled proteins. It is proposed that the ratio of protein phosphorylation to protein dephosphorylation is regulated by the ATP to ADP ratio in the cytosol. 
  Reference    Z. Naturforsch. 41c, 856 (1986); received July 9/August 5 1986 
  Published    1986 
  Keywords    Protein Kinase, Protein Phosphatase, Cytosol, Protoplasts, Pisum sativum 
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 TEI-XML for    default:Reihe_C/41/ZNC-1986-41c-0856.pdf 
 Identifier    ZNC-1986-41c-0856 
 Volume    41 
2Author    B. JanistynRequires cookie*
 Title    Effects of Adenosine-3': 5 '-monophosphate (cAMP) on the Activity of Soluble Protein Kinases in Maize {Zea mays) Coleoptile Homogenates  
 Abstract    Seven protein kinases (P I —P V II) from m aize (Zea m ays) coleoptile hom ogenates could be detected which phosphorylate a histone-substrate in a polyacrylamide-matrix. The kinases P I, PII and P V I were stim ulated by 6 ^im cA M P , P H I, P IV and P V were cAM P independent, while P V II was inhibited by 6 cAM P. 
  Reference    Z. Naturforsch. 41c, 579—584 (1986); received January 3/February 3 1986 
  Published    1986 
  Keywords    M aize, cA M P, Protein Kinases, Substrate-Inclusion Electrophoresis 
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 TEI-XML for    default:Reihe_C/41/ZNC-1986-41c-0579.pdf 
 Identifier    ZNC-1986-41c-0579 
 Volume    41 
3Author    Helmut Wombacher, Monika Reuter-SmerdkaRequires cookie*
 Title    Spectrometric and Biological Data of l,N 6-Ethenoadenosine 3',5'-Cyclic Monophosphate  
  Reference    (Z. Naturforsch. 31c, 18 [1976]; received July 12/September 25 1975) 
  Published    1976 
  Keywords    ) l, N 6-Ethenoadenosine 3', 5'-Cyclic Monophosphate, Fluorescence, Spectra, Protein Kinase 
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 TEI-XML for    default:Reihe_C/31/ZNC-1976-31c-0018.pdf 
 Identifier    ZNC-1976-31c-0018 
 Volume    31 
4Author    W. Pyerin, N. Baibach, D. Kübler, V. KinzelRequires cookie*
 Title    Protein Kinases in HeLa Cells and in Human Cervix Carcinoma  
 Abstract    Extracts of HeLa cell fractions were analyzed by DEAE-and phospho-cellulose chromatog­ raphy for their range o f cyclic AMP-dependent and -independent protein kinase activities phosphorylating histone and/or phosvitin; extractions were by phosphate buffered saline (soluble protein kinases) and the non-ionic detergent NP-40 (membrane-bound protein kinases). The soluble fraction contained (i) cyclic AMP-dependent histone kinases type I and II as evidenced by their behaviour on DEAE-cellulose and inhibition by the specific heat-and acid-stable protein kinase inhibitor (PKI) in a dose-related manner; both types I and II as well as their purified catalytic subunit also phosphorylated protamine and — with very low efficiency -casein but not phosvitin; (ii) a histone kinase (H), insensitive to cyclic AMP and PKI, also accepting protamine as substrate but not either casein or phosvitin; (iii) a phosvitin kinase (P), insensitive to cyclic AMP and PKI, which also phosphorylates casein but not histone or protamine. These four enzyme species were also found in NP-40 extracts o f 2 7 0 0 0x g residues which, however, contained further histone and phosvitin kinase activities as yet unspecified. NP-40 extracts o f the microsomal fraction possessed, besides unspecified histone and phosvitin kinase activity, only the phosvitin kinase P and appeared to be devoid of histone kinases I, II, and H. The occurrence and ratios o f the protein kinases classified suggest an ordered distribution over the diverse subcellular fractions of HeLa cells. The overall pattern of soluble and membrane-bound histone and phosvitin kinases in extracts of cervix carcinoma tissue, the in vivo correlate o f HeLa cells, closely resembled that of similar extracts of HeLa cells. HeLa cells hence appear, despite their long in vitro history, to express protein kinase activities similar to those o f their in vivo ancestors, recommending them as a subject for the study of (certain) human protein kinase systems. 
  Reference    Z. Naturforsch. 36c, 552—561 (1981); received December 4 1980/February 161981 
  Published    1981 
  Keywords    Protein Kinases, Cyclic AMP-Dependent and -Independent, HeLa Cells, Human Cervix Carcinoma, Histone, Phosvitin 
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 TEI-XML for    default:Reihe_C/36/ZNC-1981-36c-0552.pdf 
 Identifier    ZNC-1981-36c-0552 
 Volume    36