CHIMERIC PROTEIN-A PROTEIN-G AND PROTEIN-G ALKALINE-PHOSPHATASE AS REPORTER MOLECULES

Author(s): SUN, SH; Lew, AM;
Details: Publication Year 1992-07-31,Volume 152,Issue #1,Page 43-48
Journal Title: JOURNAL OF IMMUNOLOGICAL METHODS
Publication Type: Journal Article
Abstract: The IgG binding domains of staphylococcal protein A and streptococcal protein G were expressed as a chimaera using the pGEX vector which has been advocated because its fusion proteins tend to be soluble and easily isolated on immobilised glutathione. This chimaera was soluble and abundant (yield = 18 mg/l of bacterial culture) and was tested by double diffusion in agarose and by ELISA. It was found to bind IgG of all species that either parent could bind. It was superior to protein A or protein G in binding mouse Ig. A chimaera of protein G and alkaline phosphatase was also constructed and found to be soluble and abundant (yield = 20 mg/l of bacterial culture). This protein could be used as a secondary reagent in ELISA at 5-mu-g/ml for human, rabbit and mouse and at 25-mu-g/ml for sheep.
Publisher: ELSEVIER SCIENCE BV
Keywords: BINDING; ANTIBODIES; GENE
Publisher's Version: https://doi.org/10.1016/0022-1759(92)90087-A
Terms of Use/Rights Notice: Refer to copyright notice on published article.

Creation Date: 1992-07-31 12:00:00