Forskning ved Københavns Universitet - Københavns Universitet

Forside

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

Publikation: Bidrag til tidsskriftTidsskriftartikelForskningfagfællebedømt

Standard

Immunochemically identical hydrophilic and amphiphilic forms of the bovine adrenomedullary dopamine beta-hydroxylase. / Bjerrum, Ole Jannik; Helle, K B; Bock, Elisabeth Marianne.

I: Biochemical Journal, Bind 181, Nr. 1, 1979, s. 231-7.

Publikation: Bidrag til tidsskriftTidsskriftartikelForskningfagfællebedømt

Harvard

Bjerrum, OJ, Helle, KB & Bock, EM 1979, 'Immunochemically identical hydrophilic and amphiphilic forms of the bovine adrenomedullary dopamine beta-hydroxylase', Biochemical Journal, bind 181, nr. 1, s. 231-7.

APA

Bjerrum, O. J., Helle, K. B., & Bock, E. M. (1979). Immunochemically identical hydrophilic and amphiphilic forms of the bovine adrenomedullary dopamine beta-hydroxylase. Biochemical Journal, 181(1), 231-7.

Vancouver

Bjerrum OJ, Helle KB, Bock EM. Immunochemically identical hydrophilic and amphiphilic forms of the bovine adrenomedullary dopamine beta-hydroxylase. Biochemical Journal. 1979;181(1):231-7.

Author

Bjerrum, Ole Jannik ; Helle, K B ; Bock, Elisabeth Marianne. / Immunochemically identical hydrophilic and amphiphilic forms of the bovine adrenomedullary dopamine beta-hydroxylase. I: Biochemical Journal. 1979 ; Bind 181, Nr. 1. s. 231-7.

Bibtex

@article{cfdabba0b1c011df825b000ea68e967b,
title = "Immunochemically identical hydrophilic and amphiphilic forms of the bovine adrenomedullary dopamine beta-hydroxylase",
abstract = "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.",
author = "Bjerrum, {Ole Jannik} and Helle, {K B} and Bock, {Elisabeth Marianne}",
note = "Keywords: Adrenal Medulla; Animals; Antigens; Cattle; Chromaffin Granules; Chymotrypsin; Dopamine beta-Hydroxylase; Immunoelectrophoresis, Two-Dimensional; Isoenzymes; Sepharose; Thermolysin; Trypsin; Water",
year = "1979",
language = "English",
volume = "181",
pages = "231--7",
journal = "Biochemical Journal",
issn = "0264-6021",
publisher = "Portland Press Ltd.",
number = "1",

}

RIS

TY - JOUR

T1 - Immunochemically identical hydrophilic and amphiphilic forms of the bovine adrenomedullary dopamine beta-hydroxylase

AU - Bjerrum, Ole Jannik

AU - Helle, K B

AU - Bock, Elisabeth Marianne

N1 - Keywords: Adrenal Medulla; Animals; Antigens; Cattle; Chromaffin Granules; Chymotrypsin; Dopamine beta-Hydroxylase; Immunoelectrophoresis, Two-Dimensional; Isoenzymes; Sepharose; Thermolysin; Trypsin; Water

PY - 1979

Y1 - 1979

N2 - 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.

AB - 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.

M3 - Journal article

C2 - 486154

VL - 181

SP - 231

EP - 237

JO - Biochemical Journal

JF - Biochemical Journal

SN - 0264-6021

IS - 1

ER -

ID: 21607734