Title : 2,4,6-Trinitrobenzenesulfonic acid modification of the carboxyl-terminal region (C-domain) of calreticulin.

Pub. Date : 1994 Jan 12

PMID : 8190118






3 Functional Relationships(s)
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1 The role of the primary amino groups of lysine sidechains in Ca2+ binding to calreticulin was evaluated by chemical modification of the amino group with 2,4,6-trinitrobenzenesulfonic acid (TNBS). Lysine calreticulin Homo sapiens
2 In the C-domain of calreticulin, which contains the low affinity/high capacity Ca2+ binding sites, acidic residues are interspersed at regular intervals with one or more positively charged lysine and arginine residues. Lysine calreticulin Homo sapiens
3 Our results indicate that the aminogroups of the lysine sidechains in the C-domain of calreticulin have a role in the low affinity/high capacity Ca2+ binding that is characteristic of this region of the protein and which is proposed to contribute significantly to the capacity of the endoplasmic reticulum Ca2+ store. Lysine calreticulin Homo sapiens