Primary structure of bovine adrenal phenylethanolamine N-methyltransferase.
Bovine adrenal medullary phenylethanolamine N-methyltransferase (E.C. 2.1.1.28) was sequenced to determine if primary structure or post-translational processing accounts for the charged isozymes. A blocked NH2-terminus precluded amino terminal sequencing. Therefore, cyanogen bromide and tryptic peptide fragments were isolated and subjected to gas phase/gas-liquid phase sequencing. Primary structure was identified for 45% of the protein. At least two polypeptide chains exist with alternative amino acids representing conservative changes or single-base changes in amino acid codons by comparison to the cDNA sequence for the enzyme.
Wong
D L
DL
Department of Psychiatry and Behavioral Sciences, Stanford University School of Medicine, CA 94305.
Yoo
Y S
YS
Lau
K
K
Schilling
J W
JW
D000313:Adrenal Medulla / Q000201:enzymology*; D000595:Amino Acid Sequence; D000818:Animals; D002417:Cattle; D003488:Cyanogen Bromide; D004247:DNA / Q000235:genetics; D007527:Isoenzymes / Q000235:genetics / Q000302:isolation & purification; D008969:Molecular Sequence Data; D010449:Peptide Mapping; D010625:Phenylethanolamine N-Methyltransferase / Q000235:genetics* / Q000302:isolation & purification; D011499:Protein Processing, Post-Translational; D014357:Trypsin
D007527:Isoenzymes; D004247:DNA; D010625:Phenylethanolamine N-Methyltransferase; D014357:Trypsin; D003488:Cyanogen Bromide