Escherichia coli: derived murine interleukin-1 beta with N-terminus partially N alpha-acetylated.
Two forms of murine recombinant interleukin-1 beta (mrIL-1 beta) from Escherichia coli were purified by ion exchange column chromatography; each exhibited equivalent biological activity in the murine thymocyte proliferation assay. It was determined by mass spectrometry of tryptic peptides that both retained the initiating methionine but one form was N alpha-acetylated at the N-terminus.
Lischwe
M A
MA
Du Pont Merck Pharmaceutical Company, Glenolden Laboratory, Pennsylvania 19036.
Newton
R C
RC
Huang
J J
JJ
Yates
R A
RA
Breth
L A
LA
Larsen
B S
BS
D000107:Acetylation; D000595:Amino Acid Sequence; D000818:Animals; D002852:Chromatography, Ion Exchange; D004926:Escherichia coli; D007375:Interleukin-1 / Q000096:biosynthesis / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification* / Q000494:pharmacology; D008213:Lymphocyte Activation / Q000187:drug effects; D051379:Mice; D008969:Molecular Sequence Data; D011499:Protein Processing, Post-Translational; D011993:Recombinant Fusion Proteins / Q000096:biosynthesis / Q000737:chemistry / Q000302:isolation & purification / Q000494:pharmacology
D007375:Interleukin-1; D011993:Recombinant Fusion Proteins