Title : The role of arginine residues in interleukin 1 receptor binding.

Pub. Date : 1991 Dec 11

PMID : 1837236






4 Functional Relationships(s)
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1 Modification of the proteins with phenylglyoxal, an arginine-specific reagent, resulted in the loss of Type 1 IL-1 receptor binding activity. Phenylglyoxal interleukin 1 alpha Homo sapiens
2 Cyanogen bromide cleavage of phenylglyoxal modified IL-1 alpha and IL-1 beta, followed by sequencing of the peptides, revealed that arginine-12 in IL-1 alpha and arginine-4 in IL-1 beta, which occupy the same topology in the respective crystallographic structures, are the target of phenylglyoxal. Phenylglyoxal interleukin 1 alpha Homo sapiens
3 Cyanogen bromide cleavage of phenylglyoxal modified IL-1 alpha and IL-1 beta, followed by sequencing of the peptides, revealed that arginine-12 in IL-1 alpha and arginine-4 in IL-1 beta, which occupy the same topology in the respective crystallographic structures, are the target of phenylglyoxal. Phenylglyoxal interleukin 1 alpha Homo sapiens
4 Cyanogen bromide cleavage of phenylglyoxal modified IL-1 alpha and IL-1 beta, followed by sequencing of the peptides, revealed that arginine-12 in IL-1 alpha and arginine-4 in IL-1 beta, which occupy the same topology in the respective crystallographic structures, are the target of phenylglyoxal. Phenylglyoxal interleukin 1 alpha Homo sapiens