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  Preparation and characterization of nucleotide-free and metal ion-free p21 "apoprotein"

Feuerstein, J., Goody, R. S., & Wittinghofer, A. (1987). Preparation and characterization of nucleotide-free and metal ion-free p21 "apoprotein". The Journal of Biological Chemistry, 262(18), 8455-8458. Retrieved from https://pubmed.ncbi.nlm.nih.gov/3298232/.

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JBiolChem_262_1987_8455.pdf (Any fulltext), 393KB
 
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Feuerstein, Jürgen1, Author              
Goody, Roger S.1, Author              
Wittinghofer, Alfred1, Author              
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1Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society, Jahnstrasse 29, 69120 Heidelberg, DE, ou_1497712              

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 Abstract: p21 isolated under nondenaturing conditions is obtained as a complex with guanosine nucleotides and magnesium ions. We have developed a high performance liquid chromatography method which removes greater than 95% of bound nucleotide and the metal ion very rapidly under mild conditions. At the same time, p21 is purified from minor protein impurities. The protein thus prepared is thermally much less stable than the complexed p21, but can be used for studying its interaction with nucleotides and metal ions at low temperatures. The association rate constant for p21 and GDP is 1.47 X 10(6) M-1 s-1 and for GTP is 2.9 X 10(6) M-1 s-1 at 0 degree C. By using appropriately determined dissociation rate constants we have determined the binding constant for p21.GDP and p21.GTP in the presence of excess Mg2+ to be 5.7 X 10(10) M-1 and 6.0 X 10(10) M-1, respectively, at 0 degree C.

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Language(s): eng - English
 Dates: 1987-01-051987-06-25
 Publication Status: Published in print
 Pages: 4
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 Rev. Type: Peer
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Title: The Journal of Biological Chemistry
  Other : JBC
Source Genre: Journal
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Publ. Info: Baltimore, etc. : American Society for Biochemistry and Molecular Biology [etc.]
Pages: - Volume / Issue: 262 (18) Sequence Number: - Start / End Page: 8455 - 8458 Identifier: ISSN: 0021-9258
CoNE: https://pure.mpg.de/cone/journals/resource/954925410826_1