Abstract
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.
| Original language | English |
|---|---|
| Pages (from-to) | 975-979 |
| Number of pages | 5 |
| Journal | Journal of biochemistry |
| Volume | 94 |
| Issue number | 3 |
| DOIs | |
| Publication status | Published - 1983 Jul |
ASJC Scopus subject areas
- Biochemistry
- Molecular Biology
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Cite this
Sagami, H., & Ogura, K. (1983). Multiple forms of isopentenyl pyrophosphate isomerase of avian liver. Journal of biochemistry, 94(3), 975-979. https://doi.org/10.1093/oxfordjournals.jbchem.a134441