Biomedical subjects

E Samuelsson

Publications and source records attributed to E Samuelsson.

21 records · Page 2Linked to original sources

PubMed1991

Characterization of an extended form of recombinant human insulin-like growth factor II.

To investigate the biological role of variants of human insulin-like growth factor II (IGF-II), an extended form designated IGF-IIE21, with a molecular mass of 9.8 kDa, was produced in Escherichia coli as a stable and soluble secreted fusion protein. After site-specific cleavage of the affinity purified fusion protein, followed by purification using ion exchange and reversed phase chromatography, it could be demonstrated that IGF-IIE21 and IGF-II have similar or identical activities according to radioimmunoassay and radioreceptor assay. However, IGF-IIE21 showed only 1% growth promotion activity as compared with IGF-II in a clonal expansion assay using human K562 cells which lacks IGF-I receptors. These results suggest that this extended variant of IGF-II can bind to the receptor but has limited growth promoting activity.

Amino Acid Sequence↗

PubMed1991

Facilitated in vitro refolding of human recombinant insulin-like growth factor I using a solubilizing fusion partner.

We describe a new approach to refolding recombinant proteins in which an affinity fusion partner, consisting of two IgG-binding domains (ZZ) derived from staphylococcal protein A, is used to solubilize misfolded molecules before, during and after reduction and reoxidation. We show that human insulin-like growth factor I (IGF-I) can be refolded as a fusion protein at a concentration as high as 1-2 mg/ml without the use of denaturing agents. A process scheme suitable for large scale application is described in which the yield of correctly folded human IGF-I with full biological activity is substantially increased.

Immunoglobulin G↗

PubMed1980

A general method, employing arsenazo III in liposomes, for study of calcium ionophores: results with A23187 and prostaglandins.

Multilamellar (MLV) and large unilamellar (LUV) lipid vesicles (liposomes) trap the metallochromic dye arsenazo III [2,7-bis(arsonophenylazo)-1,8-dihydroxynaphthalene-3,6-disulfonic acid ] in their aqueous compartments. When ionophore A23187 was preincorporated into either MLV or LUV above 0.001 mol%, addition of Ca to the outside of liposomes produced spectral shifts characteristic of the Ca . AIII2 complex. The method permitted detection of two molecules of A23187 per liposome. Liposomes with A23187 were permselective: divalent cations were translocated in the order Mn greater than Ca greater than Sr greater than Mg congruent to Ba. Because prostaglandins (PGs) may act as Ca ionophores, we have incorporated into MLVs and LUVs stable prostaglandins (PGE2, PGI2, PGB1), endoperoxide analogs, and a water-soluble, polymeric derivative of PGB1:PGBx. None acted as ionophore. In contrast, when added to the outside of preformed MLV or LUV, PGBx, at concentrations above 1 micro M, provoked permselective uptake of Ca equivalent to that induced by 10 nM A23187. These studies demonstrate not only that liposomes containing arsenazo III may be employed in a sensitive asssay for agents that translocate divalent cations, but that a water-soluble derivative of a naturally occurring fatty acid, PGBx, is a potent ionophore.

Arsenazo III↗