Dolichos biflorus agglutinin receptors in mouse muscle. II. Biochemical properties in relation to molecular forms of acetylcholinesterase.
A biochemical analysis has been performed on the relationship between the receptors for Dolichos biflorus agglutinin (DBA) and collagen tailed acetylcholinesterase (16S AChE) in mouse skeletal muscle. The molecular forms of AChE were separated by differential salt extraction and by gradient centrifugation. DBA binding activity was measured using a microtiter plate binding assay and affinity chromatography. The 16S form of AChE was bound to DBA, whereas globular forms of AChE were not. However, only a small proportion of 16S AChE was capable of binding to DBA, and most of the DBA binding capacity in muscle extracts was not associated with the 16S AChE. The possible association with the neuromuscular synapse of DBA binding molecules other than 16S AChE is discussed with respect to our previous histochemical study on DBA binding sites in mouse muscle.
Kaupmann
K
K
Developmental Biology Unit, University of Bielefeld/Federal Republic of Germany.
Jockusch
H
H
D000110:Acetylcholinesterase / Q000378:metabolism*; D000818:Animals; D002038:Bungarotoxins / Q000378:metabolism; D051379:Mice; D008807:Mice, Inbred BALB C; D008968:Molecular Conformation; D024510:Muscle Development; D009132:Muscles / Q000378:metabolism*; D011975:Receptors, Mitogen / Q000378:metabolism*
D002038:Bungarotoxins; C027654:Dolichos biflorus lectin receptor; D011975:Receptors, Mitogen; D000110:Acetylcholinesterase