| Literature DB >> 1830475 |
R A Williamson1, M A Persson, D R Burton.
Abstract
A human anti-(rhesus D) antibody (IgG1 lambda) Fab fragment was cloned from an Epstein-Barr-virus-transformed cell line and expressed in Escherichia coli with the use of bacteriophage lambda vectors. The cloned protein is active in binding to human erythrocytes and permits the development of a recombinant reagent for the prevention of haemolytic disease of the newborn. The method offers a rapid and effective means of rescuing human Fabs from potentially unstable cell lines secreting human antibodies.Entities:
Mesh:
Substances:
Year: 1991 PMID: 1830475 PMCID: PMC1151271 DOI: 10.1042/bj2770561
Source DB: PubMed Journal: Biochem J ISSN: 0264-6021 Impact factor: 3.857