A natural variant of bovine dopamine beta-monooxygenase with phenylalanine as residue 208: purification and characterization of the variant homo- and heterotetramers of (F208)4 and (F208)2(L208)2.
Bovine dopamine beta-monooxygenase was purified from each of 18 individual adrenal glands by the method we have developed for the rapid purification of the enzyme from a single adrenal gland. Differential peptide mapping of the 18 enzyme preparations following fluorescence labeling of their cysteine residues revealed the presence of a novel variant with Phe as residue 208 in 14 adrenal glands; seven of them were homozygous for the variant allele and the remaining seven heterozygous. The variant enzyme was a tetramer and exhibited kinetic and structural properties similar to those of the wild-type tetramer (L208)4. These results indicate an allelic polymorphism and codominant expression of the two alleles of the enzyme gene.
Narita
M
M
Department of Urology, Shiga University of Medical Science, Ohtsu, Japan.
Ishida
T
T
Tomoyoshi
T
T
Nozaki
M
M
Horiike
K
K
D000313:Adrenal Medulla / Q000201:enzymology*; D000483:Alleles; D000595:Amino Acid Sequence; D000818:Animals; D002417:Cattle; D002942:Circular Dichroism; D004299:Dopamine beta-Hydroxylase / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification* / Q000378:metabolism; D004591:Electrophoresis, Polyacrylamide Gel; D014644:Genetic Variation; D007700:Kinetics; D008969:Molecular Sequence Data; D008970:Molecular Weight; D010449:Peptide Mapping; D010641:Phenotype; D010649:Phenylalanine / Q000032:analysis* / Q000737:chemistry; D011110:Polymorphism, Genetic; D011487:Protein Conformation
D010649:Phenylalanine; D004299:Dopamine beta-Hydroxylase