Literature DB >> 4249975

Correlations of length and volume measurements in myofibril suspensions.

D R Kominz.   

Abstract

Instrumentation has been developed for the rapid electronic sizing of large numbers of myofibrils. The response of myofibrils in the presence of ATP to changes in Ca(++) concentration was examined. Shortening of myofibrils upon addition of Ca(++) was accompanied by an increased protein effective volume of approximately 10-40%. Whereas ATPase activation and increased turbidity of myofibrils upon addition of Ca(++) were reversible upon subsequent addition of EGTA, the shortening and swelling were irreversible. It is proposed that the swelling may result from the breaking of hydrophobic bonds within myosin. The ATPase activity and turbidity are measures of the input, while the shortening and swelling are measures of the output of a coupled nonequilibrium process; failure of reversal of the output indicates an uncoupling under the experimental conditions.

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Year:  1971        PMID: 4249975      PMCID: PMC1484026          DOI: 10.1016/S0006-3495(71)86194-5

Source DB:  PubMed          Journal:  Biophys J        ISSN: 0006-3495            Impact factor:   4.033


  30 in total

1.  DETERMINATION OF SWELLING AND DISINTEGRATION OF MITOCHONDRIA WITH AN ELECTRONIC PARTICLE COUNTER.

Authors:  J M GEBICKI; F E HUNTER
Journal:  J Biol Chem       Date:  1964-02       Impact factor: 5.157

2.  VOLUME CHANGES IN ISOLATED MYOFIBRILS.

Authors:  R J BASKIN
Journal:  Biochim Biophys Acta       Date:  1964-11-29

3.  The effects of adenosine triphosphate on the fibre volume of a muscle homogenate.

Authors:  B B MARSH
Journal:  Biochim Biophys Acta       Date:  1952-09

4.  The pressure developed in muscle during contraction.

Authors:  A V Hill
Journal:  J Physiol       Date:  1948-09-30       Impact factor: 5.182

5.  Interaction of actomyosin with adenosine triphosphate at low ionic strength. II. Factors influencing clearing and superprecipitation: adenosine triphosphatase and birefringence of flow studies.

Authors:  K MARUYAMA; J GERGELY
Journal:  J Biol Chem       Date:  1962-04       Impact factor: 5.157

6.  The myosin filament. I. Structural organization from antibody staining observed in electron microscopy.

Authors:  F A Pepe
Journal:  J Mol Biol       Date:  1967-07-28       Impact factor: 5.469

7.  The modification of actomyosin by alpha-actinin. II. The effect of alpha-actinin upon contractility.

Authors:  E J Briskey; K Seraydarian; W F Mommaerts
Journal:  Biochim Biophys Acta       Date:  1967-04-11

8.  Studies of adenosine triphosphatase activity and turbidity in myofibril and actomyosin suspensions.

Authors:  D R Kominz
Journal:  Biochemistry       Date:  1970-04-14       Impact factor: 3.162

9.  Low-angle x-ray diffraction studies of living striated muscle during contraction.

Authors:  G F Elliott; J Lowy; B M Millman
Journal:  J Mol Biol       Date:  1967-04-14       Impact factor: 5.469

10.  Nuclear magnetic resonance evidence using D2O for structured water in muscle and brain.

Authors:  F W Cope
Journal:  Biophys J       Date:  1969-03       Impact factor: 4.033

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  3 in total

Review 1.  How vision begins: an odyssey.

Authors:  Dong-Gen Luo; Tian Xue; King-Wai Yau
Journal:  Proc Natl Acad Sci U S A       Date:  2008-07-16       Impact factor: 11.205

2.  A note on the evolution of the transducer mechanism of the vertebrate retinal rod.

Authors:  C J Duncan
Journal:  Experientia       Date:  1977-10-15

3.  The state of water in muscle tissue as determined by proton nuclear magnetic resonance.

Authors:  R Cooke; R Wien
Journal:  Biophys J       Date:  1971-12       Impact factor: 4.033

  3 in total

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