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  • Title: Determination of the cross-linked residues in homo-dimerization of S19 ribosomal protein concomitant with exhibition of monocyte chemotactic activity.
    Author: Nishiura H, Tanase S, Sibuya Y, Nishimura T, Yamamoto T.
    Journal: Lab Invest; 1999 Aug; 79(8):915-23. PubMed ID: 10462029.
    Abstract:
    When S19 ribosomal protein molecules are intermolecularly cross-linked by a transglutaminase-catalyzed reaction, the monocyte chemotactic activity is newly expressed. Heparin, at a concentration of 1 U/ml, greatly augmented the cross-linking reaction. This augmentation was due to binding affinity of S19 ribosomal protein to heparin. The major heparin-binding region of S19 ribosomal proteins was identified to Lys23-Lys-Ser-Gly-Lys-Leu-Lys29, using region-directed mutant proteins. The amino acid residues of S19 ribosomal protein used for the intermolecular cross-linkage were then determined by the peptide map analysis with amino acid sequencing and by the site-directed mutagenesis; Gln137 and Lys122 were used in the intermolecular cross-linkage.
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