Purification of a 38-kDa protein from rabbit reticulocyte lysate which promotes protein renaturation by heat shock protein 70 and its identification as δ-aminolevulinic acid dehydratase and as a putative DnaJ protein

Journal of Biological Chemistry

Volumn 274, Issue 5, 1999, Pages 3125-3134

  Gross, Martin ^a   Hessefort, Suzanne ^a   Olin, Annette ^a  

^a UNIVERSITY OF CHICAGO   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMINOLEVULINIC ACID; CELL PROTEIN; HEAT SHOCK PROTEIN 70; PORPHOBILINOGEN; PORPHOBILINOGEN SYNTHASE; ZINC;

AMINO ACID SEQUENCE; ANIMAL CELL; ARTICLE; ENZYME ACTIVITY; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN PURIFICATION; RABBIT; RENATURATION; RETICULOCYTE LYSATE; STRUCTURE ACTIVITY RELATION;

AMINO ACID SEQUENCE; ANIMALS; CONSENSUS SEQUENCE; ELECTROPHORESIS, POLYACRYLAMIDE GEL; HEAT; HEAT-SHOCK PROTEINS; HSP40 HEAT-SHOCK PROTEINS; HSP70 HEAT-SHOCK PROTEINS; HUMANS; HYDROGEN-ION CONCENTRATION; LUCIFERASES; MICE; MOLECULAR SEQUENCE DATA; MOLECULAR WEIGHT; PORPHOBILINOGEN SYNTHASE; PROTEIN DENATURATION; RABBITS; RATS; RETICULOCYTES;

ANIMALIA; HUMULUS; ORYCTOLAGUS CUNICULUS;

EID: 0033614022     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.274.5.3125     Document Type: Article

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