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Small Peptide Interacting with Pollen Calmodulinand their Effects on Cellular Functions

Small Peptide Interacting with Pollen Calmodulin and their Effects on Cellular Functions
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摘要 The interaction between dansyl-labeled pollen calmodulin (D-pCaM) and synthesized peptides was studied in the presence of Ca2+ by fluorescence spectra. It is Found that Gly/L-Ala --> D-Ala substitution in peptide chains caused great changes in their affinity for pCaM. Besides. our data provided evidence on the dissimilarity of different CaMs although they have highly-conserved structures. A preliminary study was carried out on the effects of CaM-binding peptides on cellular signal transduction, cell proliferation, showing the participation of CaM in cell functions mentioned above. The interaction between dansyl-labeled pollen calmodulin (D-pCaM) and synthesized peptides was studied in the presence of Ca2+ by fluorescence spectra. It is Found that Gly/L-Ala --> D-Ala substitution in peptide chains caused great changes in their affinity for pCaM. Besides. our data provided evidence on the dissimilarity of different CaMs although they have highly-conserved structures. A preliminary study was carried out on the effects of CaM-binding peptides on cellular signal transduction, cell proliferation, showing the participation of CaM in cell functions mentioned above.
出处 《Chinese Chemical Letters》 SCIE CAS CSCD 1999年第11期929-932,共4页 中国化学快报(英文版)
关键词 pollen calmodulin AFFINITY cellular signal transduction cell proliferation pollen calmodulin affinity cellular signal transduction cell proliferation
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