In:
FEBS Letters, Wiley, Vol. 240, No. 1-2 ( 1988-11-21), p. 133-138
Abstract:
Single molecules of glycogen phosphorylase b exhibit images in the electron microscope which are similar in shape and dimension to those derived from X‐ray crystallography. Phosphorylase a exhibits tetramers but shows dimers in the presence of glucose. Glycogen debranching enzyme appears as a monomer with an unusual crescent or shrimp‐like shape, with occasional isologous aggregation to circular dimers. The longest dimension of the monomer is very similar to that of the phosphorylase dimer, 11.5 nm. Strong binding of the debranching enzyme to glycogen is readily visualized in the electron microscope. It is suggested that the distinctive shape of the debranching enzyme may be related to its catalytic function.
Type of Medium:
Online Resource
ISSN:
0014-5793
,
1873-3468
DOI:
10.1016/0014-5793(88)80354-5
Language:
English
Publisher:
Wiley
Publication Date:
1988
detail.hit.zdb_id:
1460391-3
SSG:
12
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