Literature DB >> 6838552

Binding of concanavalin A to calf brain synaptic vesicles.

P E March, E R Thornton.   

Abstract

Concanavalin A was employed as a tool to investigate the organization of synaptic vesicle glycoproteins. The lectin was incubated in the presence of both intact and Triton X-100 treated calf brain synaptic vesicles. Electrophoresis of treated membranes clearly demonstrated that the majority of Concanavalin A binding sites was not exposed in intact synaptic vesicles. The vesicles were isolated by the procedure of DeLorenzo and Freedman (DeLorenzo, R. J., and Freedman, S. D. (1978) Biochem. Biophys. Res. Commun. 80, 183-192). However, an extra centrifugation step at 55,000 g was required to obtain plain vesicles nearly free from coated vesicles and membrane fragments.

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Year:  1983        PMID: 6838552     DOI: 10.1016/0006-291x(83)91033-1

Source DB:  PubMed          Journal:  Biochem Biophys Res Commun        ISSN: 0006-291X            Impact factor:   3.575


  4 in total

1.  The high-molecular-weight proteins of bovine brain plain synaptic vesicles.

Authors:  P E March; E Antonian; D M Schneider; D M Rothwarf; E R Thornton
Journal:  Neurochem Res       Date:  1987-07       Impact factor: 3.996

2.  A 38,000-dalton membrane protein (p38) present in synaptic vesicles.

Authors:  R Jahn; W Schiebler; C Ouimet; P Greengard
Journal:  Proc Natl Acad Sci U S A       Date:  1985-06       Impact factor: 11.205

3.  Lectin target cells in human central nervous system and the pituitary gland.

Authors:  K Schwechheimer; G Weiss; P Schnabel; P Möller
Journal:  Histochemistry       Date:  1984

4.  Concanavalin A binding and neuronal differentiation. A light microscopic study on neuronal tumours.

Authors:  K Schwechheimer; G Weiss; P Möller
Journal:  Virchows Arch A Pathol Anat Histopathol       Date:  1984
  4 in total

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