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Molecular Pharmacology

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Research ArticleArticle

A Speciflc Soluble Protein from the Catecholamine Storage Vesicles of Bovine Adrenal Medulla

I. Purification and Chemical Characterization

W. JAMES SMITH and NORMAN KIRSHNER
Molecular Pharmacology January 1967, 3 (1) 52-62;
W. JAMES SMITH
Departments of Biochemistry and Experimental Surgery, Duke University Medical Center, Durham, North Carolina 27706
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NORMAN KIRSHNER
Departments of Biochemistry and Experimental Surgery, Duke University Medical Center, Durham, North Carolina 27706
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Abstract

The soluble proteins obtained by osmotic lysis of time catecholamine storage vesicles have been purified by chromatography on DEAE-cellulose and Sephadex G-200. The major protein fraction (S1) appears to be highly purified: it sedimented as a single homogeneous fraction in the ultracentrifuge; it gave, with few exceptions, a single protein spot upon electrophoresis at different pH values, and its amino acid composition and fingerprints of tryptic digests were constant from preparation to preparation. Immunological and enzymic analysis of this protein indicated that it contained less than 1% of highly immunogenic contaminants, one of which was dopamine-β-oxidase.

In addition to the major protein fraction, two other protein peaks were obtained from the Sephadex G-200 column. One of these (S2) appeared homogeneous in the ultracentrifuge and had an S25,w of 1.4 at a protein concentration of 3 mg/ml. This fraction was less pure than S1.

Studies of the amino acid composition, fingerprints of tryptic digests and the molecular weight of S1 indicate that the protein may consist of two identical subunits having a molecular weight of 40,000. Time data are consistent with a unit structure of (a) a single peptide chain with one intrachain disulfide bond, or (b) two or more different chains with one intra- or one interchain disulfide bond.

Studies of time binding capacity of S1 showed that it did not, by itself, or in the presence of Mg++ and ATP, bind sufficient amounts of catecholamines to be able to account for the stability of a significant fraction of the catecholamines within the storage vesicles.

ACKNOWLEDGMENT This work was supported by a grant (AM-05427) from the National Institutes of Health.

  • Copyright ©, 1967, by Academic Press Inc.

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Molecular Pharmacology
Vol. 3, Issue 1
1 Jan 1967
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Research ArticleArticle

A Speciflc Soluble Protein from the Catecholamine Storage Vesicles of Bovine Adrenal Medulla

W. JAMES SMITH and NORMAN KIRSHNER
Molecular Pharmacology January 1, 1967, 3 (1) 52-62;

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Research ArticleArticle

A Speciflc Soluble Protein from the Catecholamine Storage Vesicles of Bovine Adrenal Medulla

W. JAMES SMITH and NORMAN KIRSHNER
Molecular Pharmacology January 1, 1967, 3 (1) 52-62;
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