Affinity chromatography of viral DNA polymerases on pyran-sepharose. | Zendy

Jack G. Chirikjian | Zendy; L. A. Rye | Zendy; Takis S. Papas | Zendy

AI Assistant Blog Pricing

Home ZAIA Blog

Open Access

Affinity chromatography of viral DNA polymerases on pyran-sepharose.

Author(s) -

Jack G. Chirikjian,

L. A. Rye,

Takis S. Papas

Publication year - 1975

Publication title -

proceedings of the national academy of sciences

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 5.011

H-Index - 771

eISSN - 1091-6490

pISSN - 0027-8424

DOI - 10.1073/pnas.72.3.1142

Subject(s) - sepharose , affinity chromatography , nuclease , polymerase , dna polymerase , biochemistry , cyanogen bromide , dna , sodium dodecyl sulfate , biology , gel electrophoresis , chromatography , chemistry , microbiology and biotechnology , enzyme , gene , peptide sequence

Pyran covalently linked to cyanogen bromide-activated Sepharose has been shown to be an effective affinity matrix for several viral DNA polymerases. Differential salt elution of viral compared with cellular polymerases, as well as substrate elution, suggests the affinity nature for the matrix. Unlike some other affinity systems described, pyran-Sepharose is totally resistant to nuclease digestion and is stable at 4 degrees for several months. DNA polymerases isolated from several viruses by detergent treatment were recovered in good yield. Analysis of iodinated proteins by sodium dodecyl sulfate-gel electrophoresis revealed that the DNA polymerase of avian myeloblastosis virus found in crude preparations of the virus could be purified nearly to homogeneity by a single passage through the column. These results suggest that pyran-Sepharose is an effective affinity column that is potentially adaptable as part of a general purification procedure for viral DNA polymerases.

The content you want is available to Zendy users.

Already have an account? Click here to sign in.

Having issues? You can contact us here

Accelerating Research