Multiple isoforms of myofibrillar proteins in crustacean muscle: evidence for two slow fiber types

Conference · Wed Jan 01 00:00:00 EST 1986

OSTI ID:5009402

Mykles, D L

Four distinct patterns of myofibrillar proteins, extracted from fast and slow muscles of the lobster, Homarus americanus, are distinguished by different assemblages of regulatory and contractile protein variants. Multiple isoforms of troponin-T, -I, and -C, paramyosin, and myosin light chains occur in six muscles of the claws and abdomen. Analysis of glycerinated fibers from the claws of lobster and land crab, Gecarcinus lateralis, show that more than one isoform is expressed in a single fiber, forming unique assemblages by which subgroups can be discriminated within the broader categories of fast and slow fibers. 9 refs., 3 figs.

• Research Organization: Oak Ridge National Lab., TN (USA); Colorado State Univ., Fort Collins (USA). Dept. of Zoology
• DOE Contract Number: AC05-84OR21400
• OSTI ID: 5009402
• Report Number(s): CONF-860785-2; ON: DE87001817
• Resource Relation: Conference: International symposium on adaptive mechanisms of muscle, Szeged, Hungary, 6 Jul 1986; Other Information: Portions of this document are illegible in microfiche products
• Country of Publication: United States
• Language: English

Related Subjects

59 BASIC BIOLOGICAL SCIENCES
TROPOMYOSIN
ISOENZYMES
BIOLOGICAL LOCALIZATION
ELECTROPHORESIS
LOBSTERS
MUSCLES
ANIMALS
AQUATIC ORGANISMS
ARTHROPODS
CRUSTACEANS
DECAPODS
INVERTEBRATES
550200* - Biochemistry