The structure and evolution of parvalbumins. I. Amino acid compositional studies of parvalbumins from four perciform species.
1. Parvalbumins were isolated from the white muscle of Cynoscion regalis, Leiostomus xanthurus, and Menticirrhus americanus of the Sciaenidae and Pomatomus saltatrix of the Pomatomidae. 2. Menticirrhus contains three isoparvalbumins. The other species contain two isoparvalbumins which are designated "fast" and "slow" in accord with their electrophoretic mobilities. Measurements of the denatured molecular weights show the "slow" isoparvalbumins have slightly larger apparent molecular weights, but all apparent molecular weights are in the range 10,400-14,000. 3. Amino acid compositional studies indicate that the fast and slow isoparvalbumins in these fish represent two distinct evolutionary lineages which appear to be evolving at different rates.
D000596:Amino Acids / Q000032:analysis*; D000818:Animals; D004589:Electrophoresis, Disc; D005399:Fishes; D008970:Molecular Weight; D009124:Muscle Proteins / Q000032:analysis*; D013045:Species Specificity
D000596:Amino Acids; D009124:Muscle Proteins