Expression of Recombinant Bovine β-Lactoglobulin in Escherichia coli(Microbiology & Fermentation Industry)

スポンサーリンク

概要

• 論文の詳細を見る

• Bovine β-lactoglobulin A was expressed in Escherichia coli in its mature form. The gene was constructed using a cDNA clone which coded for amino acid residues Leu-11 to Ile-162 and a synthetic oligonucleotide coding for the initial 10 amino acids preceded by a translational start. The met-β-lactoglobulin was expressed using a tac promoter vector, pTTQ18, and accounted for approximately 15% of the total cellular protein. The recombinant met-β-lactoglobulin migrated with the same molecular weight as native β-lactoglobulin A on SDS-PAGE. The majority of the met-β-lactoglobulin produced was found in an insoluble form but could be solubilized using guanidine-HCl. The renatured preparation was >80 % pure and migrated similarly to purified β-lactoglobulin A under nondenaturing conditions.

• 社団法人日本農芸化学会の論文
• 1990-04-23

著者

• Batt Carl

  Department Of Food Science Cornell University

• Kinsella J

  Department Of Food Science Cornell University

• RABSON Laurel

  Department of Food Science, Cornell University

• WONG Dominic

  Department of Food Science, Cornell University

• KINSELLA John

  Department of Food Science, Cornell University

• Wong Dominic

  Department Of Food Science Cornell University:(present Office)usda-wrrc

• Rabson Laurel

  Department Of Food Science Cornell University:(present Office)school Of Medicine Suny-stony Brook

関連論文

• Expression and Secretion of Thaumatin from Aspergillus oryzae(Microbiology & Fermentation Industry)
• Expression of Recombinant Bovine β-Lactoglobulin in Escherichia coli(Microbiology & Fermentation Industry)

スポンサーリンク