Immunochemically identical hydrophilic and amphiphilic forms of the bovine adrenomedullary dopamine beta-hydroxylase

Research output: Contribution to journalJournal articleResearchpeer-review

By means of a monospecific antibody, dopamine beta-hydroxylase was monitored immunoelectrophoretically in various extracts of chromaffin granules. Approximately one-third of the dopamine beta-hydroxylase present was located in the membrane fraction and could only be liberated with detergent. The dopamine beta-hydroxylases of the buffer and membrane fractions were antigenically identical, but differed in their amphiphilicity, as demonstrated by the change in precipitation patterns on removal of Triton X-100 from the gel, on charge-shift crossed immunoelectrophoresis and on crossed hydrophobic interaction immunoelectrophoresis with phenyl-Sepharose. Furthermore, immunoelectrophoretic analysis in the presence of Triton X-100 plus the cationic detergent cetyltrimethylammonium bromide indicates additional heterogeneity of the membrane-bound dopamine-beta-hydroxylase. By limited proteolysis with chymotrypsin and thermolysin the amphiphilic form could be convered into its hydrophilic counterpart.
Original languageEnglish
JournalBiochemical Journal
Issue number1
Pages (from-to)231-7
Number of pages6
Publication statusPublished - 1979

Bibliographical note

Keywords: Adrenal Medulla; Animals; Antigens; Cattle; Chromaffin Granules; Chymotrypsin; Dopamine beta-Hydroxylase; Immunoelectrophoresis, Two-Dimensional; Isoenzymes; Sepharose; Thermolysin; Trypsin; Water

ID: 21607734