Affordable Access

Publisher Website

The particulate half-cystine-rich copper protein of newborn liver. Relationship to metallothionein and subcellular localization in non-mitochondrial particles possibly representing heavy lysosomes

Authors
Journal
Biochemical and Biophysical Research Communications
0006-291X
Publisher
Elsevier
Publication Date
Volume
56
Issue
3
Identifiers
DOI: 10.1016/0006-291x(74)90656-1
Disciplines
  • Biology

Abstract

Abstract The particulate half-cystine-rich copper protein of newborn liver can be partially purified by centrifugation of the heavy mitochondrial fraction through glycogen-sucrose or sucrose density gradients. The resulting sediments contained about 4% copper, about 20% half-cystine and a 2 to 3-fold increase in β-glucuronidase specific activity. The copper protein is not a true mitochondrial constituent and the data are consistent with its localization in a distinct population of heavy lysosomes. The amino acid composition of the polypeptide isolated from the crude insoluble copper protein is strikingly similar to that of metallothionein, suggesting that the neonatal protein represents a copper-rich form of metallothionein.

There are no comments yet on this publication. Be the first to share your thoughts.