Literature DB >> 1744247

Isolation and characterization of parvalbumins from skeletal muscles of a tropical amphibian, Leptodactylus insularis.

C Gerday1, P Goffard, S R Taylor.   

Abstract

Parvalbumins were isolated from skeletal muscles of a tropical amphibian, Leptodactylus insularis, and three new isotypes were identified. The total concentration of parvalbumins in L. insularis was the same as the total amounts found in an amphibian from the temperate or variable zone (Rana temporaria). Muscles of the thigh and foreleg had the maximum parvalbumin concentration (0.35 mmol.kg wet weight-1). Samples from pectoralis and rectus abdominis muscles had significantly less (0.29 mmol.kg-1). Three previously unknown parvalbumin isotypes (IV, IIIa, and IIIb) were isolated from the tropical amphibian. They were different from the isotypes (IVa and IVb) predominant in R. temporaria skeletal muscle. Parvalbumins are thought to have a role in the short-term removal of myoplasmic Ca2+ during muscle relaxation. Hence, the unique isotypes in L. insularis may reflect optimal molecular adaptations retained during the animal's evolution in a constantly warm environment.

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Year:  1991        PMID: 1744247     DOI: 10.1007/bf00257902

Source DB:  PubMed          Journal:  J Comp Physiol B        ISSN: 0174-1578            Impact factor:   2.200


  19 in total

1.  Proceedings: The possible role of parvalbumins in the control of contraction.

Authors:  C Gerday; J M Gillis
Journal:  J Physiol       Date:  1976-06       Impact factor: 5.182

Review 2.  Relaxation of vertebrate skeletal muscle. A synthesis of the biochemical and physiological approaches.

Authors:  J M Gillis
Journal:  Biochim Biophys Acta       Date:  1985-06-03

Review 3.  Evolutionary diversification of structure and function in the family of intracellular calcium-binding proteins.

Authors:  M Goodman; J F Pechère; J Haiech; J G Demaille
Journal:  J Mol Evol       Date:  1979-11       Impact factor: 2.395

4.  Energetic aspects of muscle contraction.

Authors:  R C Woledge; N A Curtin; E Homsher
Journal:  Monogr Physiol Soc       Date:  1985

5.  Carp muscle calcium-binding protein. II. Structure determination and general description.

Authors:  R H Kretsinger; C E Nockolds
Journal:  J Biol Chem       Date:  1973-05-10       Impact factor: 5.157

6.  Thermodynamic analysis of calcium binding to frog parvalbumin.

Authors:  S J Smith; R C Woledge
Journal:  J Muscle Res Cell Motil       Date:  1985-12       Impact factor: 2.698

7.  The participation of parvalbumins in the activation-relaxation cycle of vertebrate fast skeletal-muscle.

Authors:  J F Pechère; J Derancourt; J Haiech
Journal:  FEBS Lett       Date:  1977-03-15       Impact factor: 4.124

8.  Parvalbumins from the lungfish (Protopterus dolloi).

Authors:  C Gerday; B Joris; N Gerardin-Otthiers; S Collin; G Hamoir
Journal:  Biochimie       Date:  1979       Impact factor: 4.079

9.  A calorimetric study of Ca2+ binding by the parvalbumin of the toad (Bufo): distinguishable binding sites in the molecule.

Authors:  M Tanokura; M Imaizumi; K Yamada
Journal:  FEBS Lett       Date:  1986-12-01       Impact factor: 4.124

10.  Effect of tetanus duration on the free calcium during the relaxation of frog skeletal muscle fibres.

Authors:  M B Cannell
Journal:  J Physiol       Date:  1986-07       Impact factor: 5.182

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  1 in total

1.  Fast calcium removal during single twitches in amphibian skeletal muscle fibres.

Authors:  C Caputo; P Bolaños; A L Escobar
Journal:  J Muscle Res Cell Motil       Date:  1999-08       Impact factor: 2.698

  1 in total

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