Mutation of any site of N-linked glycosylation accelerates the in vivo clearance of recombinant rabbit antithrombin

Thrombosis Research

Volumn 99, Issue 4, 2000, Pages 407-415

  Ni, Hongyu ^a   Blajchman, Morris A ^a   Ananthanarayanan, Vettai S ^a   Smith, Ian J ^a   Sheffield, William P ^a  

^a MCMASTER UNIVERSITY   (Canada)

Author keywords

Antithrombin; Clearance; Glycosylation; Mutagenesis; Rabbit; Recombinant protein

Indexed keywords

ANTITHROMBIN; RECOMBINANT PROTEIN;

ANIMAL CELL; ARTICLE; COMPARATIVE STUDY; CONTROLLED STUDY; GENETIC CODE; GENETIC TRANSFECTION; NONHUMAN; PLASMA CLEARANCE; PLASMA HALF LIFE; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN GLYCOSYLATION; PROTEIN TRANSPORT; RABBIT; RNA TRANSLATION; SITE DIRECTED MUTAGENESIS;

AMINO ACID SUBSTITUTION; ANIMALS; ANTICOAGULANTS; ANTITHROMBINS; ASPARAGINE; CHO CELLS; CRICETINAE; ELECTROPHORESIS; GLYCOSYLATION; HALF-LIFE; HUMANS; MUTAGENESIS, SITE-DIRECTED; MUTATION; RABBITS; RECOMBINANT PROTEINS; TRANSFECTION;

EID: 0034663089     PISSN: 00493848     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0049-3848(00)00263-2     Document Type: Article

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