
doi: 10.1007/bf01732515
pmid: 1159797
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.
Molecular Weight, Species Specificity, Fishes, Animals, Muscle Proteins, Amino Acids, Electrophoresis, Disc
Molecular Weight, Species Specificity, Fishes, Animals, Muscle Proteins, Amino Acids, Electrophoresis, Disc
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