HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Ludwig, A. Articles by Hilz, H. Search for Related Content PubMed PubMed Citation Articles by Ludwig, A. Articles by Hilz, H. Social Bookmarking                      What's this?

J. Biol. Chem., Vol. 263, Issue 15, 6993-6999, 05, 1988

Immunoquantitation and size determination of intrinsic poly(ADP-ribose) polymerase from acid precipitates. An analysis of the in vivo status in mammalian species and in lower eukaryotes

A Ludwig, B Behnke, J Holtlund and H Hilz
Institut fur Physiologische Chemie, Universitats-Krankenhaus Eppendorf, West Germany.

Antibodies against pig thymus poly(ADP-ribose) polymerase were obtained with enzyme-hemocyanin conjugates and used for immunoquantitation. The quick-blot procedure used allowed the determination of amounts as low as 1 ng of enzyme from whole cell trichloracetic acid precipitates. When applied to analysis of various human, rodent, and bovine cell types, surprisingly similar amounts of polymerase were found (1-5 ng of pig thymus polymerase equivalents/micrograms of DNA, 2 X 10(5) polymerase molecules/HeLa cell). Also, no significant difference was seen between normal and transformed cells. Polymerase tended to decline in several fibroblast cultures upon reaching confluency, which was not reflected by total polymerase activity. Divergence between total activity and immunogenic equivalents was also seen in alkylated cells and in rat liver treated with phenobarbital. Trichloroacetic acid- insoluble fractions dissolved in sodium dodecyl sulfate buffer could also be used to analyze, by Western blotting, the size distribution of poly(ADP-ribose) polymerase in vivo. Application to various cell types revealed that all mouse and rat cells tested had two immunogenic bands (116 and 98 kDa) of similar intensity. A highly conserved structure of poly(ADP-ribose) polymerase may be deduced from the existence of immunogenic and renaturable 116-kDa polypeptide bands even in the low eukaryotes Physarum polycephalum and Dictyostelium discoideum.
CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this?

This article has been cited by other articles:

				R. Alvarez-Gonzalez Genomic Maintenance: The p53 Poly(ADP-ribosyl)ation Connection Sci. Signal., December 4, 2007; 2007(415): pe68 - pe68. [Abstract] [Full Text] [PDF]

				C. von Kobbe, J. A. Harrigan, V. Schreiber, P. Stiegler, J. Piotrowski, L. Dawut, and V. A. Bohr Poly(ADP-ribose) polymerase 1 regulates both the exonuclease and helicase activities of the Werner syndrome protein Nucleic Acids Res., August 3, 2004; 32(13): 4003 - 4014. [Abstract] [Full Text] [PDF]

				W.-J. Chang and R. Alvarez-Gonzalez The Sequence-specific DNA Binding of NF-kappa B Is Reversibly Regulated by the Automodification Reaction of Poly (ADP-ribose) Polymerase 1 J. Biol. Chem., December 7, 2001; 276(50): 47664 - 47670. [Abstract] [Full Text] [PDF]

				J.-C. Ame, V. Rolli, V. Schreiber, C. Niedergang, F. Apiou, P. Decker, S. Muller, T. Hoger, J. M.-d. Murcia, and G. de Murcia PARP-2, A Novel Mammalian DNA Damage-dependent Poly(ADP-ribose) Polymerase J. Biol. Chem., June 18, 1999; 274(25): 17860 - 17868. [Abstract] [Full Text] [PDF]

				C. M. Simbulan-Rosenthal, D. S. Rosenthal, S. Iyer, A. H. Boulares, and M. E. Smulson Transient Poly(ADP-ribosyl)ation of Nuclear Proteins and Role of Poly(ADP-ribose) Polymerase in the Early Stages of Apoptosis J. Biol. Chem., May 29, 1998; 273(22): 13703 - 13712. [Abstract] [Full Text] [PDF]

				K. G. Buki, P. I. Bauer, A. Hakam, and E. Kun Identification of Domains of Poly(ADP-ribose) Polymerase for Protein Binding and Self-association J. Biol. Chem., February 17, 1995; 270(7): 3370 - 3377. [Abstract] [Full Text] [PDF]

				M. E. Smulson, V. H. Kang, J. M. Ntambi, D. S. Rosenthal, R. Ding, and C. M. G. Simbulan Requirement for the Expression of Poly(ADP-ribose) Polymerase during the Early Stages of Differentiation of 3T3-L1 Preadipocytes, as Studied by Antisense RNA Induction J. Biol. Chem., January 6, 1995; 270(1): 119 - 127. [Abstract] [Full Text] [PDF]

				T. M. C. Yung and M. S. Satoh Functional Competition between Poly(ADP-ribose) Polymerase and Its 24-kDa Apoptotic Fragment in DNA Repair and Transcription J. Biol. Chem., March 30, 2001; 276(14): 11279 - 11286. [Abstract] [Full Text] [PDF]