Refolding and purification of yeast carboxypeptidase Y expressed as inclusion bodies in Escherichia coli

Protein Expression and Purification

Volumn 22, Issue 1, 2001, Pages 101-107

  Hahm, Moon Sun ^a   Chung, Bong Hyun ^a  

^a Korea Research Institute of Bioscience and Biotechnology (KRIBB)   (South Korea)

Author keywords

[No Author keywords available]

Indexed keywords

4 AMINO BENZYLSUCCINIC ACID; AMINO ACID; BACTERIAL CELL; CARBOXY TERMINAL SEQUENCE; CARBOXYPEPTIDASE C; CELL INCLUSION; CYTOPLASM; ENZYME DENATURATION; ENZYME PURIFICATION; ENZYME STRUCTURE; FUNGAL ENZYME; GUANIDINE HYDROCHLORIDE; HISTIDINE; IMMOBILIZED METAL AFFINITY CHROMATOGRAPHY; PROTEIN FOLDING; SOLUBILIZATION;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI; SACCHAROMYCES CEREVISIAE;

EID: 0034975927     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1006/prep.2001.1418     Document Type: Article

References (17)

1. The fungal vacuole: Composition, function, and biogenesis
2. Biosynthesis of the vacuolar yeast glycoprotein carboxypeptidase Y. Conversion of the precursor into the enzyme
3. Early stages in the yeast secretory pathway are required for transport of carboxypeptidase Y to the vacuole
4. Requirement of the propeptide for in vivo formation of active yeast carboxypeptidase Y
5. Yeast carboxypeptidase Y vacuolar targeting signal is defined by four peptide amino acids
6. Secretion and overproduction of carboxypeptidase Y by a Saccharomyces cerevisiae ssl1 mutant strain
7. Process development for high-level secretory production of carboxypeptidase Y by Saccharomyces cerevisiae
8. In vitro activation of yeast pro-carboxypeptidase y expressed as inclusion bodies in Escherichia coli
9. Simple approach to secretory production of human parathyroid hormone in Saccharomyces cerevisiae
10. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
11. A unique activity assay for carboxypeptidase A in human serum
12. Use of carboxypeptidase Y propeptide as a fusion partner for expression of small polypeptide in Escherichia coli
13. Propeptide of carboxypeptidase Y provides a chaperone-like function as well as inhibition of the enzyme activity
14. Refolding of carboxypeptidase Y folding intermediate in vitro by low-affinity binding of the proregion
15. Isolation of carboxypeptidase Y by affinity chromatography
16. Yeast carboxypeptidase Y requires glycosylation for efficient intracellular transport, but not for vacuolar sorting, in vivo stability, or activity