caa a22 4500 477101003 CHVBK 20180405111541.0 cr unu---uuuuu 170330e19960401xx s 000 0 eng 10.1007/BF00262636 doi (NATIONALLICENCE)springer-10.1007/BF00262636 Extracellular calmodulin-binding proteins in plants: purification of a 21-kDa calmodulin-binding protein [Elektronische Daten] [Tang Jun, Wu Shupin, Bai Juan, Sun Daye] A 21-kDa calmodulin (CaM)-binding protein and a 19-kDa calmodulin-binding protein were detected in 0.1 M CaCl2 extracts of Angelica dahurica L. suspension-cultured cells and carrot (Daucus carota L.) suspension-cultured cells, respectively, using a biotinylated cauliflower CaM gel-overlay technique in the presence of 1 mM Ca2+. No bands, or very weak bands, were shown on sodium dodecyl sulfate-polyacrylamide gel electrophoresis gels overlayed with biotinylated cauliflower CaM when 1 mM Ca2+ was replaced by 5 mM EGTA, indicating that the binding of these two CaM-binding proteins to CaM was dependent on Ca2+. Less 21-kDa CaM-binding protein was found in culture medium of Angelica dahurica suspension cells; however, a 21-kDa protein was abundant in the cell wall. We believe that the 21-kDa CaM-binding protein is mainly in the cell wall of Angelica dahurica. Based on its reaction with periodic acid-Schiff (PAS) reagent, this 21-kDa protein would appear to be a glycoprotein. The 21-kDa CaM-binding protein was purified by a procedure including Sephadex G-100 gel filtration and CM-Sepharose cation-exchange column chromatography. The purity reached 91% according to gel scanning. The purified 21-kDa CaM-binding protein inhibited the activity of CaM-dependent NAD kinase and the degree of inhibition increased with augmentation of the 21-kDa protein, which appeared to be the typical characteristic of CaM-binding protein. Springer-Verlag, 1996 Angelica nationallicence Calmodulin-binding protein nationallicence Extracellular glycoprotein nationallicence CaM : calmodulin nationallicence CM : carboxymethyl nationallicence NADK : NAD kinase nationallicence NC : nitrocellulose nationallicence PAS : periodic acid-Schiff nationallicence Jun Tang Biology Department, Hebei Normal University, (050016), Shijiazhuang, Hebei Province, P.R. of China aut Shupin Wu Biology Department, Hebei Normal University, (050016), Shijiazhuang, Hebei Province, P.R. of China aut Juan Bai Biology Department, Hebei Normal University, (050016), Shijiazhuang, Hebei Province, P.R. of China aut Daye Sun Biology Department, Hebei Normal University, (050016), Shijiazhuang, Hebei Province, P.R. of China aut Planta Springer-Verlag 198/4(1996-04-01), 510-516 0032-0935 198:4<510 1996 198 425 https://doi.org/10.1007/BF00262636 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1007/BF00262636 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Jun Tang Biology Department, Hebei Normal University, (050016), Shijiazhuang, Hebei Province, P.R. of China aut NATIONALLICENCE 700 1- Shupin Wu Biology Department, Hebei Normal University, (050016), Shijiazhuang, Hebei Province, P.R. of China aut NATIONALLICENCE 700 1- Juan Bai Biology Department, Hebei Normal University, (050016), Shijiazhuang, Hebei Province, P.R. of China aut NATIONALLICENCE 700 1- Daye Sun Biology Department, Hebei Normal University, (050016), Shijiazhuang, Hebei Province, P.R. of China aut NATIONALLICENCE 773 0- Planta Springer-Verlag 198/4(1996-04-01), 510-516 0032-0935 198:4<510 1996 198 425 Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer