Sialic acid residues inhibit proteolytic degradation of dopamine β‐hydroxylase
- 7 April 1980
- journal article
- Published by Wiley in FEBS Letters
- Vol. 112 (2), 195-198
- https://doi.org/10.1016/0014-5793(80)80178-5
Abstract
No abstract availableThis publication has 17 references indexed in Scilit:
- Role of carbohydrate in biological function of the adhesive glycoprotein fibronectin.Proceedings of the National Academy of Sciences, 1979
- The role of glycosylation on the biosynthesis, degradation, and secretion of the acth‐β‐lipotropin common precursor and its peptide productsFEBS Letters, 1978
- Evidence that most of the dopamine β-hydroxylase is not membrane bound in purified large dense cored noradrenergic vesiclesNeuroscience, 1978
- Composition and biogenesis of complex carbohydrates of ox adrenal chromaffin granulesNeuroscience, 1977
- Peptide chain conformation and the glycosylation of glycoproteinsBiochemical and Biophysical Research Communications, 1977
- The composition of adrenal chromaffin granules: An assessment of controversial resultsNeuroscience, 1976
- [39] Adrenal chromaffin granules: Isolation and disassemblyMethods in enzymology, 1974
- The Role of Surface Carbohydrates in the Hepatic Recognition and Transport of Circulating GlycoproteinsAdvances In Enzymology and Related Subjects Of Biochemistry, 1974
- Dopamine-β-Hydroxylase: A Tetrameric GlycoproteinProceedings of the National Academy of Sciences, 1973
- Rapid automatic analysis of sugar components of glycoproteinsAnalytical Biochemistry, 1969