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Recombinant type I regulatory subunit of the cAMP‐dependent protein kinase is biologically active
Author(s) -
Oehen Stephan,
Parsons JoAnne,
Jans David A.,
Hemmings Brian A.
Publication year - 1987
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(87)80873-6
Subject(s) - recombinant dna , protein subunit , protein kinase a , complementary dna , biochemistry , amino acid , microbiology and biotechnology , affinity chromatography , chemistry , biology , kinase , gene , enzyme
The cDNA for the porcine type I regulatory subunit (R I ) of the cAMP‐dependent protein kinase (cAMP‐PK) was cloned into two different bacterial expression vectors: pKK223 and pUC18. Recombinant R I was produced by bacteria transformed with either construct, and purified by affinity chromatography. Both the native R I from the pKK223 construct and the R I with an amino terminal extension of eight amino acids from the pUC18 construct were found to be completely native with regard to inhibition of the catalytic subunit activity and cAMP binding.

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