• Corpus ID: 6342008

Purification and properties of geranylgeranyl-diphosphate synthase from bovine brain.

@article{Sagami1994PurificationAP,
  title={Purification and properties of geranylgeranyl-diphosphate synthase from bovine brain.},
  author={Hiroshi Sagami and Y Morita and Kyozo Ogura},
  journal={The Journal of biological chemistry},
  year={1994},
  volume={269 32},
  pages={
          20561-6
        }
}
Geranylgeranyl-diphosphate synthase was purified to homogeneity from bovine brain in a one-step procedure employing an affinity column. For the construction of the affinity column, a farnesyl diphosphate analog, O-(6-amino-1-hexyl)-P-farnesylmethyl phosphonophosphate, was synthesized and linked to the spacer of the matrix of Affi-Gel 10 via the amino group. The native enzyme appeared to be a homooligomer (150-195 kDa) with a molecular mass of the monomer of 37.5 kDa. The pI for the enzyme was 6… 
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