Literature DB >> 1081585

Activation of phosphorylase in frog muscle as determined by contractile activity.

W F Mommaerts, K Vegh, E Homsher.   

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.

Entities:  

Mesh:

Substances:

Year:  1975        PMID: 1081585      PMCID: PMC2226220          DOI: 10.1085/jgp.66.5.657

Source DB:  PubMed          Journal:  J Gen Physiol        ISSN: 0022-1295            Impact factor:   4.086


  3 in total

1.  Characterization of myosin heavy chain by cyanogen bromide peptide maps.

Authors:  W F Mommaerts; K Vegh; K Seraydarian; K Meier; D Rittschof
Journal:  J Muscle Res Cell Motil       Date:  1982-06       Impact factor: 2.698

2.  Fructose 2,6-bisphosphate in rat skeletal muscle during contraction.

Authors:  Y Minatogawa; L Hue
Journal:  Biochem J       Date:  1984-10-01       Impact factor: 3.857

3.  Glycogen metabolism and the function of fast and slow muscles of the rat.

Authors:  E Villa Moruzzi; E Bergamini; Z G Bergamini
Journal:  Pflugers Arch       Date:  1981-10       Impact factor: 3.657

  3 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.