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Preliminary study on the physiological function of extracellular 21 kD calmodulin-binding protein from Angelica dahurica

Mao Guohong, Tang Wenqiang, Sun Daye

Laboratory of Molecular Cell Biology,Hebei Normal University.Shijiazhuang 050016,Hebei

Abstract

The 21 kD calmodulin-binding protein (CaMBP) was purified from extracellular extracts of suspension-cultured cells of Angelica dahurica. There was only one band either in SDS-PAGE or in IEF. Its isoelectric point is pH8.9. The purity of the 21 kD CaMBP obtained was shown to be over 94% by gel scanning. The antibody against 21 kD CaMBP was prepared by immunizing rat against ascites. Western blotting showed that the antibody was specific to 21 kD CaMBP. The addition of purified 21 kD CaMBP to the cultured medium of suspension-cultured cells of Angelica dahurica inhibited cell proliferation, whereas its antibody accelerated cell proliferation. Although the regulation of extracellular CaM activity might be complicated, the above results suggest that 21 kD CaMBP may act as a factor regulating the activation and deactivation of extracellular CaM by binding to or dissociating from it.

Key words: Angelica dahurica;Extracellular calmodulin binding protein;Purification;Antibody preparation;Cell proliferation

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Citing This Article：

Mao Guohong, Tang Wenqiang, Sun Daye. Preliminary study on the physiological function of extracellular 21 kD calmodulin-binding protein from Angelica dahurica. Acta Physiol Sin 1999; 51 (2): (in Chinese with English abstract).