High-level expression of biologically active chicken prolactin in E. coli

Takeshi Ohkubo, Minuro Tanaka, Kunio Nakashima, Kiyoshi Shimada, Noboru Saito, Koji Sato

Research output: Contribution to journalArticlepeer-review

8 Citations (Scopus)


1. 1. A large quantity of chicken prolactin (cPRL) was produced by manipulating the cPRL cDNA clone and an expression vector pKK223-3. To augment the production of the hormonal protein in E. coli, in addition to the potent tac promoter, a unique DNA linker containing a pair of Shine-Dalgarno sequences and a short preceding cistron sequence was inserted into adjacent 5'-region of the coding region. 2. 2. In sodium dodecyl sulfate polyacrylamide gel electrophoresis analysis, recombinant cPRL protein exhibited a molecular mass of 23 kDa. 3. 3. The recombinant cPRL showed equivalent binding kinetics to an antiserum raised against turkey PRL. Also, this product increased the weight of pigeon crop sac mucosa to a degree comparable to that induced by turkey PRL. 4. 4. These results indicate that this recombinant cPRL has immunological and biological activities identical to those of authentic avian PRL.

Original languageEnglish
Pages (from-to)123-128
Number of pages6
JournalComparative Biochemistry and Physiology -- Part A: Physiology
Issue number1
Publication statusPublished - May 1993
Externally publishedYes

ASJC Scopus subject areas

  • Physiology


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