Title : Purification and biochemical characterization of the complete structure of a proteolytically modified beta-2-microglobulin with biological activity.

Pub. Date : 1987 Feb 16

PMID : 3028795






3 Functional Relationships(s)
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Protein Name
Organism
1 Amino acid analysis of m-beta-2-m revealed that the protein is missing one lysine residue compared to the composition deduced from the cDNA sequence of beta-2-m. Lysine beta-2-microglobulin Homo sapiens
2 Thus proteolytic cleavage of beta-2-m in the intrachain disulphide loop releases the amino acid Lys-58, which results in a modified form of beta-2-m with a molecular mass of 11,620 Da as determined by amino acid analysis. Lysine beta-2-microglobulin Homo sapiens
3 Thus proteolytic cleavage of beta-2-m in the intrachain disulphide loop releases the amino acid Lys-58, which results in a modified form of beta-2-m with a molecular mass of 11,620 Da as determined by amino acid analysis. Lysine beta-2-microglobulin Homo sapiens