Back to Search
Start Over
Rapid, high-yield isolation of human chromogranin A from chromaffin granules of pheochromocytomas.
- Source :
-
Neuropeptides [Neuropeptides] 1992 Aug; Vol. 22 (4), pp. 235-40. - Publication Year :
- 1992
-
Abstract
- Chromogranin A (CgA) is a useful probe of human neuroendocrine neoplasia and exocytotic sympathoadrenal activity, but the application of CgA immunoassays has not been widespread because of limited availability of purified human CgA. Here we describe a rapid, high yield isolation of human CgA. After obtaining and lysing pheochromocytoma chromaffin granules, the soluble core proteins (chromogranins) were depleted of dopamine-beta-hydroxylase by passage over a concanavalin A-Sepharose affinity column, then lyophilized, resuspended in volatile buffer, and gel filtered on Sephacryl S-300. SDS-PAGE-analyzed column fractions contained homogeneous human CgA, which was verified structurally (N-terminal amino acid sequence) and immunologically (radioimmunoassay and immunoblot). The overall 22.6 mg yield of purified CgA represented 5.7% of the starting vesicle core protein. This preparation will be useful in evaluating the sympathoadrenal system and endocrine neoplasia in man.
- Subjects :
- Adrenal Gland Neoplasms ultrastructure
Amino Acid Sequence
Chromatography, Affinity
Chromatography, Gel
Chromogranin A
Chromogranins chemistry
Electrophoresis, Polyacrylamide Gel
Humans
Immunoblotting
Microscopy, Electron
Molecular Sequence Data
Pheochromocytoma ultrastructure
Adrenal Gland Neoplasms chemistry
Chromaffin Granules chemistry
Chromogranins isolation & purification
Pheochromocytoma chemistry
Subjects
Details
- Language :
- English
- ISSN :
- 0143-4179
- Volume :
- 22
- Issue :
- 4
- Database :
- MEDLINE
- Journal :
- Neuropeptides
- Publication Type :
- Academic Journal
- Accession number :
- 1508327
- Full Text :
- https://doi.org/10.1016/0143-4179(92)90052-x