The engineered, cytosolic form of human type I 3β-hydroxysteroid dehydrogenase/isomerase: Purfication, characterization and crystallization

Journal of Molecular Endocrinology

Volumn 27, Issue 1, 2001, Pages 77-83

  Thomas, J L ^a   Mason, J I ^a   Blanco, G ^a   Veisaga, M L ^a  

^a MERCER UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

3(OR 17)BETA HYDROXYSTEROID DEHYDROGENASE; AMINO ACID; COMPLEMENTARY DNA; DETERGENT; DODECYL SULFATE SODIUM; HISTIDINE; HYDROXYAPATITE; MEMBRANE PROTEIN; NICOTINAMIDE ADENINE DINUCLEOTIDE; PRASTERONE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE; SODIUM CHLORIDE; TYROSINE;

AFFINITY CHROMATOGRAPHY; ALLOSTERISM; ANIMAL CELL; ARTICLE; BACULOVIRUS; CENTRIFUGATION; CONTROLLED STUDY; CRYSTALLIZATION; CYTOSOL; ENZYME ACTIVITY; ENZYME MODIFICATION; ENZYME PURIFICATION; ENZYME STRUCTURE; ENZYME SUBSTRATE; GENE DELETION; GENE EXPRESSION; GENETIC ENGINEERING; HUMAN; MICHAELIS CONSTANT; MICROSOME; MITOCHONDRION; MOLECULAR WEIGHT; NONHUMAN; POLYACRYLAMIDE GEL ELECTROPHORESIS; POLYMERASE CHAIN REACTION; PRIORITY JOURNAL; SITE DIRECTED MUTAGENESIS;

CHROMATOGRAPHY, GEL; CRYSTALLIZATION; CYTOSOL; ELECTROPHORESIS, POLYACRYLAMIDE GEL; HUMANS; KINETICS; MULTIENZYME COMPLEXES; MUTAGENESIS, SITE-DIRECTED; PROGESTERONE REDUCTASE; PROTEIN ENGINEERING; RECOMBINANT PROTEINS; STEROID ISOMERASES;

EID: 0034888720     PISSN: 09525041     EISSN: None     Source Type: Journal    
DOI: 10.1677/jme.0.0270077     Document Type: Article

References (15)

1. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
2. Inhibition of 3-beta-hydroxysteroid dehydrogenase: An approach for prostate cancer treatment?
3. Induction of 3β-hydroxysteroid dehydrogenase/isomerase type 1 expression by interleukin-4 in human normal prostate epithelial cells, immortalized keratinocytes, colon, and cervix cancer cell lines
4. 4 isomerase type 1 gene transcription in human breast cancer cell lines and in normal mammary epithelial cells by interleukin-4 and interleukin-13
5. Reproductive endocrinology
6. Functional activity of 3β-hydroxysteroid dehydrogenase/isomerase
7. Over-expression of human type I (placental) 3β-hydroxy-5-ene-steroid dehydrogenase/isomerase in insect cells infected with recombinant baculovirus
8. + isomerase gene family
9. Human placental 3β-hydroxy-5-ene-steroid dehydrogenase and steroid 5-4-ene-isomerase: Purification from microsomes, substrate kinetics and inhibition by product steroids
10. Human placental 3β-hydroxy-5-ene-steroid dehydrogenase and steroid 5-4-ene-isomerase: Purification from mitochondria and kinetics profiles, biophysical characterization of the purified mitochondrial and microsomal enzymes
11. Site-directed mutagenesis identifies amino acid residues associated with the dehydrogenase and isomerase activities of human type I (placental) 3β-hydroxysteroid dehydrogenase/isomerase
12. Creation of a fully active, cytosolic form of human type I 3β-hydroxysteroid dehydrogenase/isomerase by the deletion of a membrane-spanning domain
13. A highly active, soluble mutant of the membrane-associated (S)-mandelate dehydrogenase from Pseudomonas Putida
14. Rapid purification of the over-expressed membrane 3β-hydroxysteroid dehydrogenase in the presence of detergents