Abstract
Poly(ADP-ribose) synthetase is a versatile nuclear enzyme that catalyzes all steps of poly(ADP-ribosyl)ation, i.e., initiation, elongation, and branching of poly(ADP-ribose) chains, on acceptor proteins [1–3]. The enzyme has been purified from various sources to apparent homogeneity and characterized by many investigators [2, 3]. The properties of the enzymes from different sources are almost identical, including an absolute dependency of the activity on DNA strand ends, and the capability of modifying itself (automodification) [2, 3]. We reported also that an NAD glycohydrolase activity is associated with this ADP-ribose transferring enzyme [4]. In order to investigate the mechanisms of this variety of enzyme actions, we recently immobilized the enzyme on a gel matrix [5], and analyzed its properties in comparison with free (nonimmobilized) enzyme.
This is a preview of subscription content, log in via an institution.
Buying options
Tax calculation will be finalised at checkout
Purchases are for personal use only
Learn about institutional subscriptionsPreview
Unable to display preview. Download preview PDF.
References
Ueda K, Kawaichi M, Oka J, Hayaishi O (1980) Biosynthesis and degradation of poly(ADP-ribosyl) histones. In: Smulson M, Sugimura T (eds) Novel ADP-ribosylations of regulatory enzymes and proteins. Elsevier/North-Holland, Amsterdam New York, pp 47–56
Ueda K, Kawaichi M, Hayaishi O (1982) Poly(ADP-ribose) synthetase. In: Hayaishi O, Ueda K (eds) ADP-ribosylation reactions: biology and medicine. Academic Press, New York London, pp 117–155
Ueda K, Hayaishi O (1985) ADP-ribosylation. Annu Rev Biochem 54:71–99
Kawaichi M, Ueda K, Hayaishi O (1981) NAD glycohydrolase activity of poly(ADP-ribose) synthetase. Seikagaku 53:877 (in Japanese)
Ueda K, Zhang J, Hayaishi O (1984) Poly(ADP-ribose) synthetase. Methods Enzymol 106: 500–504
Ito S, Shizuta Y, Hayaishi O (1979) Purification and characterization of poly(ADP-ribose) synthetase from calf thymus. J Biol Chem 254:3647–3651
Kawaichi M, Ueda K, Hayaishi O (1980) Initiation of poly(ADP-ribosyl) histone synthesis by poly(ADP-ribose) synthetase. J Biol Chem 255:816–819
Kawaichi M, Ueda K, Hayaishi O (1981) Multiple autopoly(ADP-ribosyl)ation of rat liver poly(ADP-ribose) synthetase. Mode of modification and properties of automodified synthetase. J Biol Chem 256:9483–9489
Chan WW-C (1977) Immobilized subunits. Methods Enzymol 44:491–503
Kameshita I, Matsuda Z, Taniguchi T, Shizuta Y (1984) Poly(ADP-ribose) synthetase. Separation and identification of three proteolytic fragments as the substrate-binding domain, the DNA-binding domain, and the automodification domain. J Biol Chem 259:4770–4776
Holtlund J, Lemtland R, Kristensen T (1983) Two proteolytic degradation products of calfthymus poly(ADP-ribose) polymerase are efficient ADP-ribose acceptors. Implications for polymerase architecture and the automodification of the polymerase. Eur J Biochem 130: 309–314
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 1985 Springer-Verlag Berlin Heidelberg
About this chapter
Cite this chapter
Ueda, K., Zhang, J., Hayaishi, O. (1985). Immobilized Poly(ADP-Ribose) Synthetase: Preparation and Properties. In: Althaus, F.R., Hilz, H., Shall, S. (eds) ADP-Ribosylation of Proteins. Proceedings in Life Sciences. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-70589-2_6
Download citation
DOI: https://doi.org/10.1007/978-3-642-70589-2_6
Publisher Name: Springer, Berlin, Heidelberg
Print ISBN: 978-3-642-70591-5
Online ISBN: 978-3-642-70589-2
eBook Packages: Springer Book Archive