An N-linked glycosylation motif from the noncleaving luteinizing hormone receptor substituted for the homologous region (Gly367 to Glu369) of the thyrotropin receptor prevents cleavage at its second, downstream site

Journal of Biological Chemistry

Volumn 272, Issue 45, 1997, Pages 28296-28300

  Kakinuma, Ayumu ^a   Chazenbalk, Gregorio D ^a   Tanaka, Kunihiko ^a   Nagayama, Yuji ^a,b   McLachlan, Sandra M ^a   Rapoport, Basil ^a,c  

^a UNIVERSITY OF CALIFORNIA   (United States)

^b NAGASAKI UNIVERSITY   (Japan)

^c SAN FRANCISCO VETERANS AFFAIRS MEDICAL CENTER   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

LUTEINIZING HORMONE RECEPTOR; THYROTROPIN RECEPTOR;

AMINO ACID SUBSTITUTION; ARTICLE; CHIMERA; MUTAGENESIS; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN GLYCOSYLATION;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ANIMALS; CATTLE; GLUTAMINE; GLYCINE; GLYCOSYLATION; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; PROTEIN CONFORMATION; RECEPTORS, LH; RECEPTORS, THYROTROPIN; RECOMBINANT FUSION PROTEINS;

EID: 0030699380     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.272.45.28296     Document Type: Article

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