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-Reference-Cited by-同舟云学术

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

Published:1999-01 Issue:5 Volume:274 Page:3125-3134
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Gross Martin,Hessefort Suzanne,Olin Annette

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference49 articles.

1. Purification and Characterization of a 66-kDa Protein from Rabbit Reticulocyte Lysate Which Promotes the Recycling of Hsp 70

2. Extensive Sequencing of Tryptic Peptides of a Rabbit Reticulocyte 66-kDa Protein That Promotes Recycling of Hsp 70

3. Molecular cloning and expression of a transformation-sensitive human protein containing the TPR motif and sharing identity to the stress-inducible yeast protein STI1.

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