[Study of calcium-binding properties of the Mts-1 protein and its recombinant analog using the fluorescent probe Fura-2].
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.
Dukhanina
E A
EA
Danish Society for Cancer Research, Kopenhagen, Denmark.
Dukhanin
A S
AS
Lukanidin
E M
EM
Georgiev
G P
GP
D002118:Calcium / Q000378:metabolism; D002135:Calcium-Binding Proteins / Q000378:metabolism*; D016257:Fura-2; D011994:Recombinant Proteins / Q000378:metabolism; D009418:S100 Proteins
D002135:Calcium-Binding Proteins; D011994:Recombinant Proteins; D009418:S100 Proteins; D002118:Calcium; D016257:Fura-2
Izuchenie kal'tsiĭsviazyvaiushchikh svoĭstv belka Mts-1 i ego rekombinantnogo analoga s pomoshch'iu fluorestsentnogo zonda Fura-2.