Probes for Examining the Structure and Function of Human S-Adenosylhomocysteine Hydrolase, and for Isolation of cDNA

  • Michael S. Hershfield
  • V. Nambi Aiyar
  • Sara Chaffee
  • Sylvia Curtis
  • Michael L. Greenberg
Chapter
Part of the Experimental Biology and Medicine book series (EBAM, volume 12)

Abstract

The catalytic activity of AdoHcy hydrolase requires formation of a stable complex with the cofactor NAD (Palmer and Abeles, 1976). In addition to NAD, Hershfield and Kredich (1978) identified AdoHcyase as the so-called ’cAMP-Ado’ or ’adenine analogue’ binding protein that had been isolated by a number of investigators (Yuh and Tao, 1974; Sugden and Corbin, 1976; Ueland and Doskeland, 1977; Olsson, 1978). The ability to form stable complexes with NAD, Ado and its analogs, and cAMP raises questions regarding the relationship of AdoHcyase to other proteins that bind these ligands, and possible functions of ligand binding, which might be related or unrelated to the role of this enzyme in metabolism.

Keywords

Solid Phase Assay cAMP Binding Adenine Arabinoside AdoHcy Hydrolase Adenine Analogue 
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

© The Humana Press Inc. 1986

Authors and Affiliations

  • Michael S. Hershfield
    • 1
  • V. Nambi Aiyar
    • 1
  • Sara Chaffee
    • 1
  • Sylvia Curtis
    • 1
  • Michael L. Greenberg
    • 1
  1. 1.Duke University Medical CenterDurhamUSA

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