Four kinds of isopentenyl pyrophosphate isomerase were separated from avian liver homogenates by DE-52 cellulose column chromatography. These enzymes were similar in terms of optimum pH (pH 6.6) and metal ion requirement (Mn2+). They all catalyzed the specific elimination of the pro-R hydrogen at C-2 of isopentenyl pyrophosphate. However, they showed different susceptibilities to iodo-acetamide and β-mercaptoethanol.
|Number of pages||5|
|Journal||Journal of biochemistry|
|Publication status||Published - 1983 Jul|
ASJC Scopus subject areas
- Molecular Biology