Isolation and characterization of a 34,000-dalton calmodulin- and F-actin-binding protein from chicken gizzard smooth muscle.
We isolated a 34,000-dalton protein from the heat-soluble fraction of avian smooth muscle using the procedures of ammonium sulfate fractionation, cation exchange chromatography and gel filtration. The amount of 34,000-dalton protein in the muscle homogenate was as much as tropomyosin. The 34,000-dalton protein bound to F-actin and F-actin-tropomyosin in a Ca2+-independent manner, but it Ca2+-dependently interacted with calmodulin. We tentatively named the 34,000-dalton protein gizzard p34K.
D000199:Actins / Q000378:metabolism; D000818:Animals; D002147:Calmodulin / Q000378:metabolism; D002148:Calmodulin-Binding Proteins / Q000302:isolation & purification* / Q000378:metabolism; D002352:Carrier Proteins / Q000302:isolation & purification* / Q000378:metabolism; D018260:Gelsolin; D000070559:Gizzard, Non-avian / Q000032:analysis*; D007526:Isoelectric Point; D008840:Microfilament Proteins; D008970:Molecular Weight; D009124:Muscle Proteins / Q000302:isolation & purification*; D009130:Muscle, Smooth / Q000032:analysis*; D011485:Protein Binding; D014335:Tropomyosin / Q000378:metabolism
D000199:Actins; D002147:Calmodulin; D002148:Calmodulin-Binding Proteins; D002352:Carrier Proteins; D018260:Gelsolin; D008840:Microfilament Proteins; D009124:Muscle Proteins; D014335:Tropomyosin; C016953:brevin; C053028:gizzard p34K protein, chicken