碱性多肽和蛋白质与钙调蛋白的相互作用。
Interactions of basic polypeptides and proteins with calmodulin.
作者信息
Itano T, Itano R, Penniston J T
出版信息
Biochem J. 1980 Sep 1;189(3):455-9. doi: 10.1042/bj1890455.
Low concentrations (less than 10 microgram/ml) of a number of highly basic polypeptides inhibit the calmodulin-stimulated cyclic nucleotide phosphodiesterase. Inhibitory compounds include synthetic polypeptides [polylysine (D and L) and polyarginine] and basic proteins (protamine, histones H1, H2A, H2B, H3 and H4 and myelin basic protein). Polylysine of mol.wt. about 2000 or higher was inhibitory, but pentalysine did not inhibit. Other basic proteins and compounds did not inhibit, including bradykinin, spermine and putrescine. In mixtures of calmodulin and basic protein, complexes were formed whether Ca2+ was present or not. This was true for polylysine, myelin basic protein and histone H2B. These interactions suggest that the inhibition of the phosphodiesterase is due to interaction of these basic proteins with calmodulin. The wide variety of basic polypeptides and proteins that affect the calmodulin stimulation of phosphodiesterase indicates that these interactions are not specific.
低浓度（低于10微克/毫升）的多种高碱性多肽可抑制钙调蛋白刺激的环核苷酸磷酸二酯酶。抑制性化合物包括合成多肽[聚赖氨酸（D型和L型）和聚精氨酸]以及碱性蛋白（鱼精蛋白、组蛋白H1、H2A、H2B、H3和H4以及髓鞘碱性蛋白）。分子量约为2000或更高的聚赖氨酸具有抑制作用，但五聚赖氨酸无抑制作用。其他碱性蛋白和化合物无抑制作用，包括缓激肽、精胺和腐胺。在钙调蛋白与碱性蛋白的混合物中，无论是否存在Ca2+，都会形成复合物。聚赖氨酸、髓鞘碱性蛋白和组蛋白H2B均是如此。这些相互作用表明，磷酸二酯酶的抑制是由于这些碱性蛋白与钙调蛋白相互作用所致。影响钙调蛋白对磷酸二酯酶刺激作用的多种碱性多肽和蛋白表明，这些相互作用并非特异性的。
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