Title : Affinity capture of a mammalian DNA polymerase beta by inhibitors immobilized to resins used in solid-phase organic synthesis.

Pub. Date : 2005 Jan-Feb

PMID : 15656580






6 Functional Relationships(s)
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Protein Name
Organism
1 Lithocholic acid (LCA), an inhibitor of pol beta, was immobilized on various solid supports, and the batch affinity purification of pol beta from a mixture of proteins using these LCA-immobilized resins was examined. Lithocholic Acid DNA polymerase beta Homo sapiens
2 Lithocholic acid (LCA), an inhibitor of pol beta, was immobilized on various solid supports, and the batch affinity purification of pol beta from a mixture of proteins using these LCA-immobilized resins was examined. Lithocholic Acid DNA polymerase beta Homo sapiens
3 Lithocholic acid (LCA), an inhibitor of pol beta, was immobilized on various solid supports, and the batch affinity purification of pol beta from a mixture of proteins using these LCA-immobilized resins was examined. Lithocholic Acid DNA polymerase beta Homo sapiens
4 Lithocholic acid (LCA), an inhibitor of pol beta, was immobilized on various solid supports, and the batch affinity purification of pol beta from a mixture of proteins using these LCA-immobilized resins was examined. Lithocholic Acid DNA polymerase beta Homo sapiens
5 Using the LCA-immobilized resin, it was possible to purify pol beta from a mixture of proteins. Lithocholic Acid DNA polymerase beta Homo sapiens
6 The pol beta inhibitors LCA, C18-beta-SQDG, and epolactaene were immobilized on the photoaffinity beads by photoreaction. Lithocholic Acid DNA polymerase beta Homo sapiens