Myosin of fast and slow muscles of the rabbit

Myosin of slow muscles of the rabbit has two or three times lower actin-activated and EDTA-activated ATPase and Ca ++-activated ATPase and ITPase activities than those of rabbit fast muscles. Unlike myosin of fast muscles, the Ca ++- and EDTA-activated ATPase activities of myosin of slow muscles are...

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Published inArchives of biochemistry and biophysics Vol. 109; no. 1; pp. 185 - 191
Main Authors Bárány, M., Bárány, K., Reckard, T., Volpe, A.
Format Journal Article
LanguageEnglish
Published United States Elsevier Inc 1965
Subjects
Adenosine Triphosphatases
Animals
Calcium
Calcium, Dietary
Denervation
Edetic Acid
Metabolism
Muscle Contraction
Muscle Proteins
Muscles
Myosins
Old Medline
Phosphoric Monoester Hydrolases
Rabbits
Ultracentrifugation
ADENOSINE TRIPHOSPHATASE
RABBITS
METABOLISM
CALCIUM
EXPERIMENTAL LAB STUDY
MUSCLE CONTRACTION
DENERVATION
MUSCLE PROTEINS
EDTA
ULTRACENTRIFUGATION
PHOSPHATASES
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Summary:Myosin of slow muscles of the rabbit has two or three times lower actin-activated and EDTA-activated ATPase and Ca ++-activated ATPase and ITPase activities than those of rabbit fast muscles. Unlike myosin of fast muscles, the Ca ++- and EDTA-activated ATPase activities of myosin of slow muscles are not increased in the alkaline pH range. Despite these qualitative differences, both kinds of muscle contain the same amount of myosin. Fast muscle contains more sarcoplasmic and less stroma proteins than slow muscle, whereas actin content is the same. After 19 days of denervation the myosin isolated from fast muscle shows only a slight decrease in its NTPase activities and no change in its pH-activity curve compared with the myosin of the same normal muscle.
Bibliography:ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
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ISSN:0003-9861
1096-0384
DOI:10.1016/0003-9861(65)90304-8