Abstract
The state of activation of phosphorylation in muscle has been reinvestigated by combining the extraction procedures of Danforth, Helmreich, and Cori with the low-temperature techniques of this laboratory. In resting frog muscle, the phosphorylase-alpha content is usually below detectability. Upon contractile activity in series of twitches, activation of phosphorylase beta to alpha took place, without activation of phosphorylase beta kinase as defined by the assay procedure. Two different experimental designs were used to examine the relation between phosphorylase activation and the myothermally determined energy turnover per twitch, and these showed, identically, that the enzyme activation is proportional to the energy per twitch.
Full Text
The Full Text of this article is available as a PDF (814.3 KB).