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Different Forms of Adrenal Phenylethanolamine N ‐Methyltransferase: Species‐Specific Posttranslational Modification
Author(s) -
Park Dong H.,
Baetge E. Edward,
Kaplan Barry B.,
Albert Vivian R.,
Reis Donald J.,
Joh Tong H.
Publication year - 1982
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/j.1471-4159.1982.tb08644.x
Subject(s) - phenylethanolamine , enzyme , phenylethanolamine n methyltransferase , biochemistry , polyacrylamide gel electrophoresis , methyltransferase , antibody , gel electrophoresis , biology , microbiology and biotechnology , in vitro , chemistry , electrophoresis , methylation , dna , tyrosine hydroxylase , immunology
Phenylethanolamine N ‐methyltransferase was purified from rat and cow adrenal glands. The enzymes from the two species have the same molecular weight of 31,000, but differ in electrophoretic mobility. During polyacrylamide gel electrophoresis, the rat form migrates faster than the bovine form. Antibodies to bovine enzyme precipitated equally well the rat and cow form of the enzyme, but antibodies against rat enzyme precipitated poorly the bovine form. In contrast, both antibodies recognized a similar protein in the in vitro translation products of poly(A + )mRNA isolated from cow adrenal glands. The results suggest that the primary protein structure of rat and bovine enzyme is similar and that differences in electrophoretic mobility are due to posttranslational modification of the enzyme molecule.