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

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

doi:10.1016/0300-9629(93)90183-5

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 journal › Article › peer-review

7 Citations (Scopus)

Abstract

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 language	English
Pages (from-to)	123-128
Number of pages	6
Journal	Comparative Biochemistry and Physiology -- Part A: Physiology
Volume	105
Issue number	1
DOIs	https://doi.org/10.1016/0300-9629(93)90183-5
Publication status	Published - May 1993
Externally published	Yes

ASJC Scopus subject areas

Physiology

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title = "High-level expression of biologically active chicken prolactin in E. coli",

abstract = "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.",

author = "Takeshi Ohkubo and Minuro Tanaka and Kunio Nakashima and Kiyoshi Shimada and Noboru Saito and Koji Sato",

year = "1993",

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T1 - High-level expression of biologically active chicken prolactin in E. coli

AU - Ohkubo, Takeshi

AU - Tanaka, Minuro

AU - Nakashima, Kunio

AU - Shimada, Kiyoshi

AU - Saito, Noboru

AU - Sato, Koji

PY - 1993/5

Y1 - 1993/5

N2 - 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.

AB - 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.

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