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The myoglobin content in red, intermediate and white fibres of the swimming muscle sin three species of shark–a comparative study using high‐performance liquid chromatography
Author(s) -
Kryvi H.,
Flatmark T.,
Flatmark T.,
Totland G. K.
Publication year - 1981
Publication title -
journal of fish biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.672
H-Index - 115
eISSN - 1095-8649
pISSN - 0022-1112
DOI - 10.1111/j.1095-8649.1981.tb03774.x
Subject(s) - myoglobin , high performance liquid chromatography , chromatography , biology , scyliorhinus canicula , gel permeation chromatography , muscle fibre , metmyoglobin , anatomy , biochemistry , chemistry , skeletal muscle , fishery , organic chemistry , fish <actinopterygii> , polymer
A high‐performance liquid chromatographic (HPLC) procedure is described for the determination of myoglobin in extracts of small samples of tissue from the three different fibre types in the swimming muscles of three species of sharks, Etmopterus spinax, Galeus melastomus and Scyliorhinus canicula . The method, which is based on the separation of myoglobin from haemoglobin from haemoglobin based on HPLC using a gel permeation chromatography column, has a detection limit of about 3 pmol myoglobin (Mb). In addition it has the added advantage of specific identification by its Soret band absorption and quantification. In all three species, the three fibre types of the muscle are completely separated and can be isolated at a high degree of purity. In red fibres the myoglobin content varied between 565 nmol mg −1 wet weight ( Scyliorhinus ) and 170 nmol mg −1 wet weight ( Galeus ). Intermediate fibres contained from 215 to 57, and white fibres from 11 to zero nmol mg −1 wet weight. The myoglobin content is closely correlated to the vascularization as well as to the amounts of mitochondria in the different fibre types.