Title: trans-Golgi retention of a plasma membrane protein: mutations in the cytoplasmic domain of the asialoglycoprotein receptor subunit H1 result in trans-Golgi retention Document date: 1995_7_2
ID: tedj3xxz_26
Snippet: Upon proteinase K digestion at 4°C, 50% of the mature form of H1 was degraded in M1 cells (normalized to the precursor form; Fig. 3, lanes 4 and 5) . This corresponded HepG2, M1, and M1A cells were incubated at 4°C or 37°C for 30 min with (PK) or without (-) proteinase K as indicated. After blocking the protease, the cells were solubilized and subjected to gel electrophoresis and immunoblot analysis using anti-ASGP receptor antiserum. Protecti.....
Document: Upon proteinase K digestion at 4°C, 50% of the mature form of H1 was degraded in M1 cells (normalized to the precursor form; Fig. 3, lanes 4 and 5) . This corresponded HepG2, M1, and M1A cells were incubated at 4°C or 37°C for 30 min with (PK) or without (-) proteinase K as indicated. After blocking the protease, the cells were solubilized and subjected to gel electrophoresis and immunoblot analysis using anti-ASGP receptor antiserum. Protection of the mature forms was quantified by densitometric scanning, and normalized to the high-mannose precursor form. The complex and high-mannose glycosylated forms of H1 are indicated by C and H, respectively.
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