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PMID: 1247586 Published · ppublish English Journal Article

Isolation and characterization of a Golgi-rich fraction from the adrenal medulla.

Biochimica et biophysica acta ·Vol. 421 ·No. 1 ·1976-01-14 ·Pages 153-67

Trifaró JM, Duerr AC

Abstract

1. A Golgi-rich fraction from bovine adrenal medulla was isolated by centrifugation through discontinuous sucrose density gradients. 2. The specific activity of UDPgalactose-N-acetylglucosamine galactosyl transferase was increased in this fraction. Therefore, this enzyme is a useful marker for Golgi in bovine adrenal medulla. 3. Golgi membranes were reasonably free from mitochondria, lysosomes, endoplasmic reticulum and chromaffin granules as shown by the relatively low activities of marker enzymes. 4. The negative staining techniques of electron microscopy revealed the presence of a system of tubules, vesicles and plate-like center regions which are similar to those structures previously described of the Golgi fraction isolated from the liver. 5. The specific activity of 5'-nucleotidase in the Golgi-rich fraction was 3.5 times greater than that in adrenal homogenates. However, the subcellular distribution patterns of galactosyl transferase and 5'-nucleotidase were similar. The possibility that 5'-nucleotidase might be a conspicious component of the Golgi apparatus is discussed.

MeSH Terms
Adrenal Medulla/enzymology,ultrastructure Animals Cattle Cell Fractionation/methods Centrifugation, Density Gradient/methods Dopamine beta-Hydroxylase/analysis Galactosyltransferases/analysis Golgi Apparatus/enzymology,ultrastructure Microscopy, Electron
Chemicals
Dopamine beta-Hydroxylase Galactosyltransferases
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Trifaró J M
Duerr A C
Article Info
Journal
Biochimica et biophysica acta
Abbr.
Biochim Biophys Acta
ISSN
0006-3002
Published
1976-01-14
Pages
153-67
Language
English
Region
Netherlands
NLM ID
0217513
Subset
IM
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