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Chunk #23 — Results — The relative molecular mass (Mr) of MOPR in G/G mice was lower than that in A/A mice, which is due to differences in N-glycosylation of MOPR

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A common single nucleotide polymorphism A118G of the μ opioid receptor alters its N-glycosylation and protein stability.
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and 2), respectively. Treatment of the WGL affinity-purified materials with PNGase F resulted in an increase in the mobility of thalamic MOPRs in both A/A and G/G mice on SDS–PAGE (Fig. 3, lanes 3 and 4), compared with the untreated controls (Fig. 3, lanes 1 and 2). More importantly, the diffuse MOPR bands with different median Mr's in the two mouse lines (Fig. 3, lanes 1 and 2) became sharp bands with a lower and identical Mr (41 kDa) (Fig. 3, lanes 3 and 4). Thus, the difference in Mr's of the MOPRs in A/A and G/G mice is due to differential N-linked glycosylation.