Structural and functional differences among purified recombinant mammalian aromatases: Glycosylation, N-terminal sequence and kinetic analysis of human, bovine and the porcine placental and gonadal isozymes

Molecular and Cellular Endocrinology

Volumn 206, Issue 1-2, 2003, Pages 147-157

  Corbin, C Jo ^a   Mapes, S M ^a   Lee, Young M ^a   Conley, Alan J ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

Androgen; Aromatase; Bovine; Difference spectroscopy; Estrogen; Glycosylation; Human; Ovary; P450; Peptide sequence; Placenta; Porcine

Indexed keywords

ANDROSTENEDIONE; AROMATASE; CYTOCHROME P450; GLYCOPROTEIN; ISOENZYME; TESTOSTERONE;

AMINO ACID SEQUENCE; AMINO TERMINAL SEQUENCE; ANIMAL CELL; ANIMAL TISSUE; ARTICLE; BINDING AFFINITY; BIODIVERSITY; CATALYSIS; CATALYST; CONTROLLED STUDY; ENZYME PURIFICATION; GLYCOSYLATION; GONAD; HUMAN; HUMAN CELL; HUMAN TISSUE; KINETICS; MOLECULAR SIZE; NONHUMAN; PLACENTAL MAMMALS; PRIORITY JOURNAL;

EID: 0042433312     PISSN: 03037207     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0303-7207(02)00422-7     Document Type: Article

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