English (United Kingdom)

https://curated-unify.zendy.io/wp-json/zendy-region/v1/featured_content/oa?rat=en

https://curated-unify.zendy.io/wp-json/zendy-region/v1/highlighted_journal/

Global: Zendy Plus annual

Presents the access of premium content as premium feature

Premium Content

Presents the keyphrase highlighting as premium feature

Keyphrase Highlighting

Presents the summarisation as premium feature

Summarisation

Insights

Presents the pdf analysis as premium feature

PDF Analysis

Presents the zaia usage as premium feature

ZAIA

Global: Zendy Plus monthly

Global: Zendy Tools annual

Global: Zendy Tools monthly

Global: Zendy Free Plan

A number of biochemical studies have been carried out in recent years on muscle affected by Eavitaminotic dystrophy in order to discover the primary biochemical changes responsible for the onset and the development of the dystrophic condition. Since 1951 Aloisi and co-workers have shown that in this condition quantitative and qualitative changes take place in the contractile proteins of rabbit muscle (see Aloisi, 1951; Aloisi, Ascenzi & Bonetti, 1953). The myosin content of musclefibre extracts decreases rapidly and actin loses its power of polymerization (Aloisi, Ascenzi & Bonetti, 1952a, b, c; Bonetti, Aloisi & Merucci, 1952). There is also other circumstantial evidence that in the dystrophic condition actin or actomyosin can be found in a depolymerized form: observations with the polarizing microscope and electronmicroscopic investigations on isolated dystrophic myofibrils (Bompiani, 1954) and on solutions of muscle proteins (Aloisi et al. 1952a) are consistent with this assumption. Also Feuer & Frigyes (1952) have found a loss of myosin in nutritional dystrophy, and Crepax (1952) has obtained the same results by electrophoretic investigations on muscle extracts. This author has also shown two gradients which are supposed to correspond to the G-actin and to the Y-protein of Dubuisson (1950). In latelactation paralysis of rats Rumery, Mauer & Mason (1955) have found a reversible decrease of a fraction of muscle proteins which seems to correspond with actomyosin. Changes in myosin and in actomyosin have also been found by Fischer (1950) in denervation atrophy. In this condition actomyosin has been reported to have a diminished capacity for contraction, and myosin is less uniform in dispersity and has decreased adenosine triphosphatase activity. The purpose of our work has been to analyse in some detail the changes of contractile proteins during the development of the dystrophy. A preliminary note on the results here presented has already been published (Azzone & Aloisi, 1955). As will be shown below, we have divided muscle

Changes induced by E-avitaminosis on the proteins of rabbit-muscle extracts