Isolation and characterization of tropomyosin from fish muscle.
A comprehensive survey of tropomyosin from various fish myotomal muscles is reported. The fish tropomyosins were blocked at the N-terminus and, as expected, were found to be of similar amino acid composition, alpha-helical content (> 90% at 10 degrees C) and molecular weight to other vertebrate striated muscle forms. The tropomyosins of salmonids and herring muscle were noticeably heterogeneous when assessed by 2D-PAGE. The distribution of isoforms was tissue-specific: slow muscle contained alpha-type tropomyosin while fast muscle contained beta-type tropomyosin. In other species (cod, haddock, wolf-fish and sharks) alpha-type tropomyosins were present in both kinds of muscle but beta-tropomyosin was absent.
Heeley
D H
DH
Department of Biochemistry, Memorial University, St John's, Newfoundland, Canada.
Hong
C
C
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002942:Circular Dichroism; D015180:Electrophoresis, Gel, Two-Dimensional; D005399:Fishes / Q000235:genetics / Q000378:metabolism*; D008969:Molecular Sequence Data; D008970:Molecular Weight; D017433:Protein Structure, Secondary; D011817:Rabbits; D013045:Species Specificity; D014335:Tropomyosin / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification*
D000596:Amino Acids; D014335:Tropomyosin