Literature DB >> 32155

A combined histochemical and biochemical study of myofibrillar ATPase in pectoral, leg and cardiac muscle of several species of bird.

G L Talesara, G Goldspink.   

Abstract

Frozen sections of the pectoral, gastrocnemius and cardiac muscles from seven different species of birds were stained for myofibrillar ATPase and for succinic dehydrogenase. Several methods of myofibrillar ATPase were used including different pre-incubation treatments. Myofibrillar ATPases were also measured biochemically and the pH profile of the activity was compared with the histochemical staining following pre-incubation at different pH. Myofibrils from the different muscles were also subjected to sodium dodecyl sulphate acrylamide gel electrophoresis in order to separate the low molecular weight components of myosin. The results demonstrated that histochemical methods can be applied, with a reasonable degree of confidence, to classifying fibres in avian muscles although the classification used for mammalian muscles needs to be modified. They also showed that avian muscles, particularly the pectoralis, varies considerably between species and their mode of locomotion.

Entities:  

Mesh:

Substances:

Year:  1978        PMID: 32155     DOI: 10.1007/bf01003119

Source DB:  PubMed          Journal:  Histochem J        ISSN: 0018-2214


  22 in total

1.  Characterization of myosin light chains from histochemically identified fibres of rabbit psoas muscle.

Authors:  A G Weeds; R Hall; N C Spurway
Journal:  FEBS Lett       Date:  1975-01-01       Impact factor: 4.124

2.  The specificity of the histochemical method for adenosine triphosphatase.

Authors:  H A PADYKULA; E HERMAN
Journal:  J Histochem Cytochem       Date:  1955-05       Impact factor: 2.479

3.  A study of the effects of substrate concentration and certain relaxing factors on the magnesium-activated myofibrillar adenosine triphosphatase.

Authors:  T C GREY; S V PERRY
Journal:  Biochem J       Date:  1956-09       Impact factor: 3.857

4.  Determination of serum proteins by means of the biuret reaction.

Authors:  A G GORNALL; C J BARDAWILL; M M DAVID
Journal:  J Biol Chem       Date:  1949-02       Impact factor: 5.157

5.  Biochemistry of adenosine triphosphatase activity of avian fast and slow muscle.

Authors:  R H Reasons; R S Hikida
Journal:  Exp Neurol       Date:  1973-01       Impact factor: 5.330

6.  Fact and artifact in the histochemical procedure for myofibrillar ATPase.

Authors:  L Guth
Journal:  Exp Neurol       Date:  1973-11       Impact factor: 5.330

Review 7.  Dynamic properties of mammalian skeletal muscles.

Authors:  R I Close
Journal:  Physiol Rev       Date:  1972-01       Impact factor: 37.312

8.  Procedure for the histochemical demonstration of actomyosin ATPase.

Authors:  L Guth; F J Samaha
Journal:  Exp Neurol       Date:  1970-08       Impact factor: 5.330

9.  Qualitative differences between actomyosin ATPase of slow and fast mammalian muscle.

Authors:  L Guth; F J Samaha
Journal:  Exp Neurol       Date:  1969-09       Impact factor: 5.330

10.  ATPase activity of myosin correlated with speed of muscle shortening.

Authors:  M Bárány
Journal:  J Gen Physiol       Date:  1967-07       Impact factor: 4.086

View more
  5 in total

1.  Modifications in the histochemical and biochemical changes in tenotomized rat soleus by denervation.

Authors:  C L Talesara; P K Jasra
Journal:  Pflugers Arch       Date:  1986-08       Impact factor: 3.657

2.  High altitude tissue adaptation in Andean coots: capillarity, fibre area, fibre type and enzymatic activities of skeletal muscle.

Authors:  F León-Velarde; J Sanchez; A X Bigard; A Brunet; C Lesty; C Monge
Journal:  J Comp Physiol B       Date:  1993       Impact factor: 2.200

3.  Myocardial cell heterogeneity in the human heart with respect to myosin ATPase activity.

Authors:  L E Thornell; S Forsgren
Journal:  Histochem J       Date:  1982-05

4.  Fibre types in chicken skeletal muscles and their changes in muscular dystrophy.

Authors:  E A Barnard; J M Lyles; J A Pizzey
Journal:  J Physiol       Date:  1982-10       Impact factor: 5.182

5.  Myosin heavy-chain isoforms in the flight and leg muscles of hummingbirds and zebra finches.

Authors:  Brandy P Velten; Kenneth C Welch
Journal:  Am J Physiol Regul Integr Comp Physiol       Date:  2014-03-26       Impact factor: 3.619

  5 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.