| pubmed-article:8754275 | pubmed:abstractText | A procedure based on the ability of Mts-1 to competitively inhibit the formation of Fura-2 complexes with Ca(2+)-ions is described. It has been shown that Mts-I reversibly inhibits the complex formation between Fura-2 and calcium. The efficiency of natural Mts-I isolated from cells of the CSML-100 line and of its recombinant analog on the formation of the Fura-2+Ca complex is different. The inhibition constant, Ki, for the native protein is equal to 2,4 microM, that for the recombinant form is 8.5 microM. The data obtained are suggestive of posttranslational modification of Mts-I in cells under in vivo conditions. | lld:pubmed |
