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