Crosslinking and binding of fibronectin with asymmetric acetylcholinesterase
- 1 May 1981
- journal article
- research article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 20 (11) , 3242-3247
- https://doi.org/10.1021/bi00514a040
Abstract
The similarities between the tail of asymmetric acetylcholinesterase [AcChE, from quail (Coturnix coturnix japonica muscle]and collagen prompted an investigation of whether asymmetric AcChE, like collagen, can interact with [human plasma] fibronectin. Gradient centrifugation studies revealed that asymmetric, but not globular, AcChE bound to fibronectin and could be cross-linked covalently to fibronectin by plasma transglutaminase. The interaction asymmetric AcChE with fibronectin paralleled the interaction of fibronectin with collagen. Fibronectin may be involved in attaching asymmetric AcChE to cell surfaces.This publication has 6 references indexed in Scilit:
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