EFFECTS OF CATIONS ON AFFINITY OF CALMODULIN FOR CALCIUM - ORDERED BINDING OF CALCIUM-IONS ALLOWS THE SPECIFIC ACTIVATION OF CALMODULIN-STIMULATED ENZYMES
EFFECTS OF CATIONS ON AFFINITY OF CALMODULIN FOR CALCIUM - ORDERED BINDING OF CALCIUM-IONS ALLOWS THE SPECIFIC ACTIVATION OF CALMODULIN-STIMULATED ENZYMES
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DOI:
10.1021/bi00516a035
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发表时间:
1981-01-01
期刊:
影响因子:
2.9
通讯作者:
DEMAILLE, JG
中科院分区:
文献类型:
--
作者:
HAIECH, J;KLEE, CB;DEMAILLE, JG
The acid stability of calmodulin was used to devise a rapid and efficient method of decalcification based on trichloroacetic acid precipitation. Study of the competitive binding of K+, Mg2+ and Ca2+ to the Ca2+-binding sites of [ram testes] calmodulin allowed determination of the intrinsic binding constants of each of the 3 cations for the 4 Ca2+-binding sites. The data are compatible with an ordered binding of Ca2+. If the Ca2+ sites are labeled A, B, C and D starting at the NH2 terminus, the order of binding is postulated to the B, A, C and D. The ordered binding properties support the suggestion that calmodulin translates quantitative Ca2+ signals into qualitatively different cellular responses.