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Studies of the Catalytically-Active Form of Hypoxanthine-Guanine Phosphoribosyltransferase from Yeast

  • Donald L. Sloan
  • Linda Z. Ali
  • Dian Picou
  • Antonio JosephJr.
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 165)

Abstract

Studies of the kinetic (1) and structural (2) properties of yeast hypoxanthine-guanine phosphoribosyltransferase (HG-PRTase), an enzyme first purified by Schmidt et al. (3), have been completed recently. This HG-PRTase is composed of two polypeptide subunits(26,000 m.w.), as determined by SDS-gel electrophoresis (2) and catalyzes the synthesis of either IMP or GMP through the use of an ordered Bi Bi kinetic mechanism (1). However, since electro-phoretic studies are conducted at concentrations much higher than those employed during kinetic analyses, the observed dimeric HG-PRTase, may not necessarily be the form of the enzyme responsible for catalysis. In this paper we describe results which suggest the existence of a catalytically-active monomeric HG-PRTase which functions as an enzyme-metal ion complex.

Keywords

Crosslinking Reagent Manganese Chloride Polypeptide Subunit High Molecular Weight Form Orotate Phosphoribosyltransferase 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Springer Science+Business Media New York 1984

Authors and Affiliations

  • Donald L. Sloan
    • 1
  • Linda Z. Ali
    • 1
  • Dian Picou
    • 1
  • Antonio JosephJr.
    • 1
  1. 1.Chemistry Dept.City College of the City University of New YorkNew YorkUSA

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