A covalently linked recombinant albumin dimer is more rapidly cleared in vivo than are wild-type and mutant C34A albumin

Journal of Laboratory and Clinical Medicine

Volumn 143, Issue 2, 2004, Pages 115-124

  Mccurdy, Teresa R ^b   Gataiance, Sharon ^b   Eltringham Smith, Louise J ^b   Sheffield, William P ^a  

^a MCMASTER UNIVERSITY   (Canada)

^b NONE

Author keywords

[No Author keywords available]

Indexed keywords

ALANINE; ALANINE DERIVATIVE; CHELATE; CYSTEINE; CYSTEINE DERIVATIVE; DISULFIDE; HISTIDINE DERIVATIVE; HYBRID PROTEIN; MUTANT PROTEIN; NICKEL; POLYPEPTIDE; PRIMER DNA; RECOMBINANT PROTEIN; SERUM ALBUMIN;

AMINO ACID SUBSTITUTION; AMINO TERMINAL SEQUENCE; ANIMAL; ARTICLE; CARBOXY TERMINAL SEQUENCE; CATABOLISM; CHEMISTRY; DIMERIZATION; DISULFIDE BOND; GEL FILTRATION CHROMATOGRAPHY; GENETICS; HALF LIFE TIME; HEART; ION EXCHANGE; KIDNEY; LIVER; LUNG; METABOLIC CLEARANCE RATE; METABOLISM; MOLECULAR CLONING; NUCLEOTIDE SEQUENCE; PICHIA; PICHIA PASTORIS; PLASMID; POLYMERASE CHAIN REACTION; PROTEIN EXPRESSION; PROTEIN LOCALIZATION; RABBIT; RADIOIODINATION; RETICULOENDOTHELIAL SYSTEM; REVERSE TRANSCRIPTION POLYMERASE CHAIN REACTION; SITE DIRECTED MUTAGENESIS; SPLEEN; URINE; WILD TYPE; YEAST;

EID: 1242294497     PISSN: 00222143     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.lab.2003.10.008     Document Type: Article

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