Enzymatic deglycosylation of the dendrotoxin‐binding protein

FEBS Letters

Rehm, Hubert¹ 

[1] VA Medical Center, GRECC 182-B, 1660 S. Columbian Way, Seattle, WA 98108, USA

关键词: Deglycosylation;    K+ channel;    Dendrotoxin;    Neuraminidase;    Glycopeptidase F;   

DOI  :  10.1016/0014-5793(89)81233-5

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The neuronal membrane protein which binds the K⁺-channel ligands dendrotoxin, mast cell degranulating peptide, and β-bungarotoxin was purified from rat brain membranes. When analysed on 10% SDS gel electrophoresis, the purified protein contained two peptides: the toxin-binding subunit of apparent M _r, 90 000 and another peptide of M _r, 38 000. Neuraminidase treatment reduced the M _r, of the toxin-binding subunit to 70 000. Glycopeptidase F gave a further reduction to M _r, 65 000. In contrast, the peptide of M _r, 38 000 showed no change in M _r, upon treatment with neuraminidase and/or glycopeptidase F. It is concluded that the toxin-binding subunit of the dendrotoxin-binding protein, a presumptive K⁺ channel, is a sialated membrane protein with a peptide core of, at most, M _r, 65 000.

【 授权许可】

Unknown