Reduction of biological activity of murine recombinant interleukin-1 beta by selective deamidation at asparagine-149.
A biologically active preparation of murine recombinant interleukin-1 beta (mIL-1 beta) from Escherichia coli cell lysates contained tow forms of mIL-1 beta with pI 8.7 and pI 8.1, respectively. Treatment with 0.1 M Tris, pH 8.5, at 37 degrees C for 35 h converted the pI 8.7 form to the pI 8.1 form by the selective deamidation of an asparagine residue (Asn149) in the mIL-1 beta molecule. Deamidated mIL-1 beta had 3- to 5-fold lower co-mitogenic activity and receptor affinity than the unmodified form.
Daumy
G O
GO
Central Research Division, Pfizer Inc., Groton, CT 06340.
Wilder
C L
CL
Merenda
J M
JM
McColl
A S
AS
Geoghegan
K F
KF
Otterness
I G
IG
D000577:Amides / Q000737:chemistry; D000595:Amino Acid Sequence; D000818:Animals; D001216:Asparagine / Q000737:chemistry*; D002852:Chromatography, Ion Exchange; D004591:Electrophoresis, Polyacrylamide Gel; D007375:Interleukin-1 / Q000378:metabolism*; D051379:Mice; D008969:Molecular Sequence Data; D011994:Recombinant Proteins / Q000378:metabolism; D013329:Structure-Activity Relationship
D000577:Amides; D007375:Interleukin-1; D011994:Recombinant Proteins; D001216:Asparagine