Weikert, T. ; Ebert, C. ; Rasched, I. ; Layer, Paul G. (1994)
Novel inactive and distinctively glycosylated forms of butyrylcholinesterase from chicken serum.
In: Journal of neurochemistry, 63 (1)
Artikel, Bibliographie
Kurzbeschreibung (Abstract)
Three different homologues of butyrylcholinesterase (BChE) with 75-, 62-, and 54-kDa subunit size are isolated from adult chicken serum, and all show very low or zero enzyme activity. Although the active BChE from serum with a subunit size of 81 kDa forms tetramers, the 75-kDa protein is isolated as a dimer. The homology of the 75-kDa protein with active BChE is shown by immunoreactivity with BChE-specific monoclonal antibodies, by coisolation with the active BChE, and by their identical first six N-terminal amino acids. By deglycosylation of these proteins and by their differential lectin binding, we show that the active BChE is an N-glycosylated protein of the triantennary type, whereas the inactive 75-kDa protein is O-glycosylated. These data show for the first time the existence of (1) multiple inactive forms of BChE, (2) secreted inactive cholinesterases, because they are found in serum, and (3) an O-glycosylated cholinesterase. Because cholinesterases can regulate neurite growth in vitro by a nonenzymatic mechanism, these data strongly support that both inactive and active forms of BChE may be involved in noncholinergic communication, possibly depending on particular glycosylation patterns.
| Typ des Eintrags: | Artikel |
|---|---|
| Erschienen: | 1994 |
| Autor(en): | Weikert, T. ; Ebert, C. ; Rasched, I. ; Layer, Paul G. |
| Art des Eintrags: | Bibliographie |
| Titel: | Novel inactive and distinctively glycosylated forms of butyrylcholinesterase from chicken serum. |
| Sprache: | Englisch |
| Publikationsjahr: | 1994 |
| Titel der Zeitschrift, Zeitung oder Schriftenreihe: | Journal of neurochemistry |
| Jahrgang/Volume einer Zeitschrift: | 63 |
| (Heft-)Nummer: | 1 |
| Kurzbeschreibung (Abstract): | Three different homologues of butyrylcholinesterase (BChE) with 75-, 62-, and 54-kDa subunit size are isolated from adult chicken serum, and all show very low or zero enzyme activity. Although the active BChE from serum with a subunit size of 81 kDa forms tetramers, the 75-kDa protein is isolated as a dimer. The homology of the 75-kDa protein with active BChE is shown by immunoreactivity with BChE-specific monoclonal antibodies, by coisolation with the active BChE, and by their identical first six N-terminal amino acids. By deglycosylation of these proteins and by their differential lectin binding, we show that the active BChE is an N-glycosylated protein of the triantennary type, whereas the inactive 75-kDa protein is O-glycosylated. These data show for the first time the existence of (1) multiple inactive forms of BChE, (2) secreted inactive cholinesterases, because they are found in serum, and (3) an O-glycosylated cholinesterase. Because cholinesterases can regulate neurite growth in vitro by a nonenzymatic mechanism, these data strongly support that both inactive and active forms of BChE may be involved in noncholinergic communication, possibly depending on particular glycosylation patterns. |
| Fachbereich(e)/-gebiet(e): | 10 Fachbereich Biologie ?? fb10_zoologie ?? 10 Fachbereich Biologie > Developmental Biology and Neurogenetics |
| Hinterlegungsdatum: | 21 Nov 2011 13:59 |
| Letzte Änderung: | 05 Mär 2013 09:56 |
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