Journal of Histochemistry and Cytochemistry Priciples for Free Access to Science
  Search:   
    >> Advanced Search

Guidelines | Subscriptions | About | exPRESS - Current - Archive | Business Information | Contact
This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by SCHIAFFINO, S.
Right arrow Articles by BORMIOLI, S. P.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by SCHIAFFINO, S.
Right arrow Articles by BORMIOLI, S. P.
Social Bookmarking
Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

HISTOCHEMICAL CHARACTERIZATION OF ADENOSINE TRIPHOSPHATASES IN SKELETAL MUSCLE FIBERS BY SELECTIVE EXTRACTION PROCEDURES

STEFANO SCHIAFFINO 1 and SANDRA PIEROBON BORMIOLI 1

1 National Research Council Unit for Muscle Biology and Physiopathology, Institute of General Pathology, University of Padova, 35100 Padova, Italy

Selective extraction procedures have been applied to frozen sections of rat skeletal muscles to determine the relative contribution of myosin adenosine triphosphatase (ATPase) and of membrane-bound (mitochondrial and sarcotubular) ATPases to the histochemical ATPase reactions demonstrated in muscle fibers by the calcium precipitatation mehod (Padykula-Herman procedure) and by the lead precipitation medium (Wachstein-Meisel procedure). A detergent treatment was used to solubilize membrane-bound enzymes and hypertonic KCl solution to extract myosin. Pretreatment with the non-ionic detergent, Triton X-100, severely depressed the ATPase activity demonstrated by the lead method, as well as several membrane-bound dehydrogenase activities, but did not affect the intensity of the ATPase reaction demonstrated in the muscle fibers by the calcium method. After detergent treatment, however, the end product of the latter reaction showed a network distribution which contrasted with the characteristic myofibrillar localization observed in untreated sections. Hypertonic KCl pretreatment, when applied to undried sections, abolished the ATPase reaction demonstrated in the muscle fibers by the calcium method; the ATPase demonstrated by the lead method was slightly depressed and the dehydrogenase activities unmodified by the same treatment. The results indicate that the ATPase activity demonstrated histochemically in skeletal muscle fibers by the calcium method is due to myosin ATPase, and suggest that the intermyofibrillar localization of the end product which occurs under certain conditions is artifactual.

Submitted on July 31, 1972


Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?





Guidelines | Subscriptions | About | exPRESS - Current - Archive | Business Information | Contact
The Journal of Histochemistry & Cytochemistry is owned, published, and licensed by The Histochemical Society © 1973