Direct visualization of phosphorylase-phosphorylase kinase complexes by scanning tunneling and atomic force microscopy

In skeletal muscle the activation of phosphorylase b is catalyzed by phosphorylase kinase. Both enzymes occur in vivo as part of a multienzyme complex. The two enzymes have been imaged by atomic force microscopy and the results compared to those previously found by scanning tunneling microscopy. Sca...

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Bibliographic Details
Published in:Biophysical journal 1990-12, Vol.58 (6), p.1437-1448
Main Authors: Edstrom, R.D., Meinke, M.H., Yang, X.R., Yang, R., Elings, V., Evans, D.F.
Format: Article
Language:English
Subjects:
Analytical, structural and metabolic biochemistry
Animals
Biological and medical sciences
complex
electron microscopy
Electron Probe Microanalysis - methods
Enzymes and enzyme inhibitors
Fundamental and applied biological sciences. Psychology
Microscopy, Scanning Tunneling - methods
Muscles - enzymology
phosphorylase
Phosphorylase b - metabolism
Phosphorylase b - ultrastructure
phosphorylase kinase
Phosphorylase Kinase - metabolism
Phosphorylase Kinase - ultrastructure
Protein Binding
Protein Conformation
Rabbits
skeletal muscle
Transferases
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Summary:In skeletal muscle the activation of phosphorylase b is catalyzed by phosphorylase kinase. Both enzymes occur in vivo as part of a multienzyme complex. The two enzymes have been imaged by atomic force microscopy and the results compared to those previously found by scanning tunneling microscopy. Scanning tunneling microscopy and atomic force microscopy have been used to view complexes between the activating enzyme phosphorylase kinase and its substrate phosphorylase b. Changes in the size and shape of phosphorylase kinase were observed when it bound phosphorylase b.
ISSN:0006-3495
1542-0086
DOI:10.1016/S0006-3495(90)82489-9