A single-step purification procedure and partial amino acid sequence analysis of picomole amounts of the rat T cell alloantigen RT6.2.
A single-step immunoaffinity purification procedure for the rat T cell marker RT6.2 is described which permits the isolation of microgram quantities of protein from the RT6.2+ T-T hybridoma EpD3. The amino terminus was sequenced directly from a polyvinylidene (PVDF) membrane blot prepared after SDS-PAGE. Further internal sequence data were obtained from peptides generated from purified RT6.2 digested with different endoproteases and separated by reverse-phase micro-HPLC. A computer search in data banks did not reveal any significant homology to other proteins.
Kashan
A
A
Dept. of Immunology, University Hospital, Hamburg, F.R.G.
Buck
F
F
Haag
F
F
Koch
F
F
Thiele
H G
HG
D036002:ADP Ribose Transferases; D000595:Amino Acid Sequence; D000818:Animals; D000945:Antigens, Differentiation, T-Lymphocyte / Q000302:isolation & purification*; D002846:Chromatography, Affinity; D002851:Chromatography, High Pressure Liquid; D006649:Histocompatibility Antigens / Q000302:isolation & purification*; D008562:Membrane Glycoproteins; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000302:isolation & purification; D051381:Rats
D000945:Antigens, Differentiation, T-Lymphocyte; D006649:Histocompatibility Antigens; D008562:Membrane Glycoproteins; D010446:Peptide Fragments; D036002:ADP Ribose Transferases; C090163:Art2b protein, rat