Literature DB >> 7925851

Dynamic laser light scattering studies of the effects of pyrophosphate on cyclic motions of cross-bridges in isolated thick myofilaments from Limulus striated muscle.

S F Fan1, M M Dewey, B Chu.   

Abstract

Pyrophosphate (PPi) is a non-hydrolyzable ATP analogue known to affect the binding between myosin heads and actin. By using a dynamic laser light scattering method, we have shown that 1-2 mM PPi enhances the increase in gamma values induced by Ca2+ in isolated thick myofilaments from Limulus striated muscle. However, similar treatment has no effect on the gamma values of filaments suspended in either relaxing solution or ATP-free solution. gamma is the average linewidth of the photoelectron count autocorrelation function of the light scattered. PPi had no effect on the increase of gamma values by Sr2+ but it substantially increased the gamma values of the thick myofilaments suspended in Ba(2+)-substituted Ca2+ activating solution. The results show that PPi also affects the energy-requiring cyclic cross-bridge motions.

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Year:  1994        PMID: 7925851     DOI: 10.1007/bf01956466

Source DB:  PubMed          Journal:  Experientia        ISSN: 0014-4754


  19 in total

1.  Effect of ionic strength on skinned rabbit psoas fibers in the presence of magnesium pyrophosphate.

Authors:  M Schoenberg
Journal:  Biophys J       Date:  1991-09       Impact factor: 4.033

2.  Ca2+-sensitive cross-bridge dissociation in the presence of magnesium pyrophosphate in skinned rabbit psoas fibers.

Authors:  B Brenner; L C Yu; L E Greene; E Eisenberg; M Schoenberg
Journal:  Biophys J       Date:  1986-12       Impact factor: 4.033

3.  The active cross-bridge motions of isolated thick filaments from myosin-regulated muscles detected by quasi-elastic light scattering.

Authors:  S F Fan; M M Dewey; D Colflesh; B Gaylinn; R A Greguski; B Chu
Journal:  Biophys J       Date:  1985-06       Impact factor: 4.033

4.  Dynamic light-scattering evidence for the flexibility of native muscle thin filaments.

Authors:  J Newman; F D Carlson
Journal:  Biophys J       Date:  1980-01       Impact factor: 4.033

5.  Quasi-elastic light scattering of suspensions of Limulus thick myofilaments in relaxed (long) activated and rerelaxed (short) states.

Authors:  K Kubota; B Chu; S F Fan; M M Dewey; P Brink; D E Colflesh
Journal:  J Mol Biol       Date:  1983-05-25       Impact factor: 5.469

6.  Cooperative binding of myosin subfragment-1 to the actin-troponin-tropomyosin complex.

Authors:  L E Greene; E Eisenberg
Journal:  Proc Natl Acad Sci U S A       Date:  1980-05       Impact factor: 11.205

7.  Quasielastic light scattering study of solutions of synthetic myosin filaments.

Authors:  N Suzuki; A Wada
Journal:  Biochim Biophys Acta       Date:  1981-10-28

8.  Half-stoichiometric trinitrophenylation of myosin subfragment 1 in the presence of pyrophosphate or adenosine diphosphate.

Authors:  H Komatsu; Y Emoto; K Tawada
Journal:  J Biol Chem       Date:  1993-04-15       Impact factor: 5.157

9.  Complexes of myosin subfragment 1 with pyrophosphate and with adenosine diphosphate as studied by phosphorus-31 nuclear magnetic resonance.

Authors:  M Tanokura; S Ebashi
Journal:  J Biochem       Date:  1993-01       Impact factor: 3.387

10.  Effect of ATP depletion on the isolated thick filament of limulus striated muscle.

Authors:  S F Fan; M M Dewey; D Colflesh; B Chu
Journal:  Biophys J       Date:  1987-11       Impact factor: 4.033

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  1 in total

Review 1.  Invertebrate muscles: thin and thick filament structure; molecular basis of contraction and its regulation, catch and asynchronous muscle.

Authors:  Scott L Hooper; Kevin H Hobbs; Jeffrey B Thuma
Journal:  Prog Neurobiol       Date:  2008-06-20       Impact factor: 11.685

  1 in total

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