Bovine thymus poly(adenosine diphosphate ribose) polymerase. Physical properties and binding to DNA.

摘要: Purified bovine thymus poly(adenosine diphosphate ribose) polymerase is a monomeric protein with single polypeptide chain having molecular weight of approximately 130,000, determined by sodium dodecyl sulfate-gel electrophoresis, analytical ultracentrifugation, and gel filtration. A high frictional ratio (1.81) indicated that the molecule has an elongated shape, or solvation, both. The enzyme basic (pI 9.8), amino acid analysis showed relatively lysine content. activity dependent on double-stranded DNA solely correlated single- breaks DNA. Filter binding assay technique enzyme-activating efficiency sufficiently its enzyme-binding efficiency. Thus, very fraction (active DNA) which was separated from crude mainly due to It also shown single-stranded heparin had strong inhibitory effect DNA, whereas competitive inhibitors did not affect binding, We interpret these results indicate prerequisite step catalytic dual function: (a) position specific sites such as (b) induce active conformation enzyme.