Purification, characterization, and partial sequence analysis of a new 25-kDa actin-binding protein from bovine aorta: a SM22 homolog.
We have purified a Ca(2+)-sensitive 25-kDa protein from bovine aorta. The 25-kDa protein remains associated with the membrane fraction in the presence of Ca2+ and is dissociated by EGTA. The purified protein binds directly to F-actin at a ratio of 1:6 actin monomers, with a binding constant of 7.0 x 10(5) M-1. The partial sequence analysis revealed a high homology to predicted protein derived from mRNA, named WS3-10 and chicken SM22 protein. Although chicken SM22 had not any interaction with contractile proteins or Ca2+, the bovine homolog clearly binds to F-actin and has Ca(2+)-binding domain in its primary structure.
Kobayashi
R
R
Department of Pharmacology, Nagoya University School of Medicine, Japan.
Kubota
T
T
Hidaka
H
H
D000199:Actins / Q000302:isolation & purification / Q000378:metabolism*; D000595:Amino Acid Sequence; D000818:Animals; D001011:Aorta / Q000378:metabolism*; D002118:Calcium / Q000378:metabolism; D002417:Cattle; D002462:Cell Membrane / Q000378:metabolism; D002645:Chickens; D004533:Egtazic Acid / Q000494:pharmacology; D006801:Humans; D007700:Kinetics; D051379:Mice; D008840:Microfilament Proteins / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism*; D008969:Molecular Sequence Data; D008970:Molecular Weight; D009124:Muscle Proteins / Q000737:chemistry; D009131:Muscle, Smooth, Vascular / Q000378:metabolism*; D009132:Muscles / Q000378:metabolism; D010446:Peptide Fragments / Q000737:chemistry; D011817:Rabbits; D017386:Sequence Homology, Amino Acid
D000199:Actins; D008840:Microfilament Proteins; D009124:Muscle Proteins; D010446:Peptide Fragments; C058992:Tagln protein, mouse; C051615:transgelin; D004533:Egtazic Acid; D002118:Calcium