Cytochemical studies of a glycogen-sarcoplasmic reticulum complex.
Enzymatically active cardiac sarcoplasmic reticulum (SR) fractions contain glycogen. Previous biochemical and morphological studies indicate that the glycogen particles are membrane associated. In the present study, further evidence for membrane-associated glycogen particles in these cardiac SR fractions is presented: (1) morphological parameters, (2) enzymatic digestion by glucoamylase and alpha-amylase and (3) cytochemical staining by two different methods. Dense granules comparable in size (20-30 nm diameter), electron density and substructure to glycogen particles observed in intact cardiac muscle and in glycogen preparations isolated from skeletal muscle were seen. Most of these glycogen particles were removed by amylase digestion except for glycogen particles closely adhering to vesicle membranes. Two different cytochemical techniques (bismuth subnitrate and silver proteinate) revealed a positive reaction product over the glycogen particles. These findings provide further support for the biochemical finding of a structured enzyme complex involving the SR, glycogenolytic enzymes and glycogen.
Goldstein
M A
MA
Murphy
D L
DL
van Winkle
W B
WB
Entman
M L
ML
D000818:Animals; D004285:Dogs; D005087:Glucan 1,4-alpha-Glucosidase / Q000378:metabolism; D006003:Glycogen / Q000032:analysis*; D006651:Histocytochemistry; D008854:Microscopy, Electron; D009206:Myocardium / Q000032:analysis*; D012519:Sarcoplasmic Reticulum / Q000032:analysis* / Q000201:enzymology; D013194:Staining and Labeling; D013347:Subcellular Fractions / Q000201:enzymology
D006003:Glycogen; D005087:Glucan 1,4-alpha-Glucosidase