title: Purification and characterization of the parvalbumin from monkey skeletal muscle.
abstract: 1. A high affinity Ca2+ binding and low mol. wt protein, parvalbumin, was purified from monkey skeletal muscle. 2. As compared with other animals, only one component and a lower content of monkey parvalbumin were found. 3. This may suggest that both the component and the content of parvalbumin decreases with biological evolution. 4. The parvalbumin was found to have a mol. wt of 11,400, a pI of 5.1, a high aspartic acid and lysine content, maximum absorption at around 260 nm, a blocked amino-terminal, an immunological distinction, 2 mol Ca2+ binding/mol, and a conformational change by Ca2+ binding. 5. Parvalbumin was shown to have alpha type properties.
authors.affiliation: Department of Biochemistry, Kyoto University, Aichi, Japan.
authors.forename: K
authors.initials: K
authors.lastname: Asaoka
authors.forename: M
authors.initials: M
authors.lastname: Tanokura
mesh_terms: D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002118:Calcium / Q000378:metabolism; D004591:Electrophoresis, Polyacrylamide Gel; D005779:Immunodiffusion; D007526:Isoelectric Point; D008251:Macaca; D008274:Magnesium / Q000378:metabolism; D008970:Molecular Weight; D009132:Muscles / Q000737:chemistry*; D010320:Parvalbumins / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism; D011487:Protein Conformation; D013056:Spectrophotometry, Ultraviolet
chemical_list: D000596:Amino Acids; D010320:Parvalbumins; D008274:Magnesium; D002118:Calcium