Premium
FOlding and Activation of Recombinant Human Prorenin
Author(s) -
Sharma SK,
Evans DB,
Tomich CS,
Cornette JC,
Ulrich RG
Publication year - 1987
Publication title -
biotechnology and applied biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.468
H-Index - 70
eISSN - 1470-8744
pISSN - 0885-4513
DOI - 10.1111/j.1470-8744.1987.tb00471.x
Subject(s) - chinese hamster ovary cell , recombinant dna , escherichia coli , in vitro , renin–angiotensin system , folding (dsp implementation) , inclusion bodies , hamster , chemistry , in vivo , protein folding , biochemistry , biology , microbiology and biotechnology , endocrinology , receptor , genetics , gene , engineering , blood pressure , electrical engineering
In vitro folding of mature renin, prorenin, and fused prorenin, all produced in denatured form in inclusion bodies in recombinant Escherichia coli, has been studied in order to evaluate the importance of prosequence in the folding of human renin. These studies have been compared with the in vivo folding and subsequent in vitro activation of recombinant human prorenin secreted by a nonbacterial expression system, namely Chinese hamster ovary (CHO) cells grown in serum‐free medium. It is concluded that prosequence is essential in the folding of human renin and, therefore, the DNA coding for this sequence cannot be removed without affecting the recovery of active human renin from recombinant bacterial and nonbacterial systems.