Identification of a thioredoxin-related protein associated with plasma membranes.
A low molecular weight membrane associated sulphydryl protein was detected on a wide range of nucleated cells when [14C]-iodoacetamide was used as a probe. This protein was extracted from THP-1 monocytes, purified to homogeneity and its isoelectric point, Mr and N-terminal amino acid sequence determined. These were shown to be almost identical to the corresponding values for both human thioredoxin and a Tac interleukin-2 receptor activator, indicating that the protein may be a member of this family and function as an essential growth factor.
Martin
H
H
Kennedy Institute of Rheumatology, London, UK.
Dean
M
M
D000595:Amino Acid Sequence; D000818:Animals; D002250:Carbon Radioisotopes; D002460:Cell Line; D002462:Cell Membrane / Q000378:metabolism; D004591:Electrophoresis, Polyacrylamide Gel; D005910:Glioma; D006168:Guinea Pigs; D006801:Humans; D007460:Iodoacetamide / Q000378:metabolism; D051379:Mice; D008807:Mice, Inbred BALB C; D008969:Molecular Sequence Data; D008970:Molecular Weight; D011485:Protein Binding; D051381:Rats; D011917:Rats, Inbred Lew; D012689:Sequence Homology, Nucleic Acid; D013879:Thioredoxins / Q000302:isolation & purification* / Q000378:metabolism
D002250:Carbon Radioisotopes; D013879:Thioredoxins; D007460:Iodoacetamide