TY - JOUR
T1 - Nonidentity of chromogranin a and dopamine β-monooxygenase
AU - Hogue-angeletti, Ruth A.
N1 - Funding Information:
1 This work was supported by grants from the National Institutes of Health, NS 13201 and NS-05572. 2 Recipient of a Public Health Service Research Career Development Award, NS-201.
PY - 1977/11
Y1 - 1977/11
N2 - Dopamine β-monooxygenase (EC 1.14.17.1) and chromogranin A from bovine adrenal chromaffin granules were purified by established procedures and examined for evidence of structural identity. The minimum molecular weights were determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and found to be 74,000 and 35,000, respectively. Amino acid analyses of the two proteins are distinct. Dopamine β-monooxygenase does not possess a free amino terminus, whereas chromogranin A has a leucine amino terminus. Analysis in the protein sequencer showed that chromogranin A contains only a single degradable polypeptide chain. Radioactive S-carboxymethyl derivatives of the two proteins were prepared to compare the soluble peptides after thermolysin digestion. These thermolytic peptides were isolated from columns of Dowex 50-X8 resin and both the peptide and radioactive traces revealed no evidence for similarity of the two proteins, either in toto or in part. Thus, although dopamine β-monooxygenase and chromogranin A may sometimes be copurified, they are distinct entities.
AB - Dopamine β-monooxygenase (EC 1.14.17.1) and chromogranin A from bovine adrenal chromaffin granules were purified by established procedures and examined for evidence of structural identity. The minimum molecular weights were determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and found to be 74,000 and 35,000, respectively. Amino acid analyses of the two proteins are distinct. Dopamine β-monooxygenase does not possess a free amino terminus, whereas chromogranin A has a leucine amino terminus. Analysis in the protein sequencer showed that chromogranin A contains only a single degradable polypeptide chain. Radioactive S-carboxymethyl derivatives of the two proteins were prepared to compare the soluble peptides after thermolysin digestion. These thermolytic peptides were isolated from columns of Dowex 50-X8 resin and both the peptide and radioactive traces revealed no evidence for similarity of the two proteins, either in toto or in part. Thus, although dopamine β-monooxygenase and chromogranin A may sometimes be copurified, they are distinct entities.
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U2 - 10.1016/0003-9861(77)90363-0
DO - 10.1016/0003-9861(77)90363-0
M3 - Article
C2 - 596880
AN - SCOPUS:0017603593
SN - 0003-9861
VL - 184
SP - 364
EP - 372
JO - Archives of Biochemistry and Biophysics
JF - Archives of Biochemistry and Biophysics
IS - 1
ER -