Abstract
A unique soluble lipoprotein has been isolated from aqueous lysates of bovine adrenal medulla chromaffin granules by DEAE-cellulose chromatography and gel filtration. Chloroform/methanol extracts of this complex contain sphingomyelin, lecithin, and cholesterol. Gel filtration in aqueous media indicates an approximate molecular weight of 900,000 for the complex. Incubation with sodium dodecyl sulfate causes dissociation to a low molecular weight polypeptide; prolonged treatment with guanidine HCl does not promote dissociation at all. Amino acid analysis revealed a high content of hydrophobic amino acids. Analysis of the tryptic fingerprint indicates that a single type of polypeptide chain is present. The complex appears to contain approximately five copies of polypeptide per aggregate.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 5613-5616 |
| Number of pages | 4 |
| Journal | Journal of Biological Chemistry |
| Volume | 253 |
| Issue number | 16 |
| State | Published - 1978 |
ASJC Scopus subject areas
- Biochemistry
- Molecular Biology
- Cell Biology