Purification and point-mutation analysis of human interleukin-2 (Ser-125).
A new type of IL-2(Ser-125) was purified by semi-preparative RP-HPLC, and its purity was analyzed with microbore HPLC, IEF, SDS-PAGE and capillary electrophoresis (CE). The N-terminal sequencing indicated the microheterogeneity of the N-terminus, i.e., N-Met(2/3) and N-Ala(1/3), which was identified with the results of CE and IEF. The amino acid sequence of the point mutated peptide confirmed the replacement of Cys-125 with Ser.
Wu
G
G
Shanghai Institute of Biochemistry, CAS, China.
Tu
H
H
Shao
X
X
Xu
L
L
Xia
Q
Q
D000595:Amino Acid Sequence; D002851:Chromatography, High Pressure Liquid; D004591:Electrophoresis, Polyacrylamide Gel; D006801:Humans; D007376:Interleukin-2 / Q000235:genetics* / Q000302:isolation & purification; D007525:Isoelectric Focusing; D008969:Molecular Sequence Data; D010449:Peptide Mapping; D017354:Point Mutation; D012694:Serine / Q000235:genetics*
D007376:Interleukin-2; D012694:Serine