The primary structure of human secretogranin II, a widespread tyrosine-sulfated secretory granule protein that exhibits low pH- and calcium-induced aggregation-Reference-Cited by-同舟云学术

The primary structure of human secretogranin II, a widespread tyrosine-sulfated secretory granule protein that exhibits low pH- and calcium-induced aggregation

Published:1989-07 Issue:20 Volume:264 Page:12009-12015
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Gerdes H H,Rosa P,Phillips E,Baeuerle P A,Frank R,Argos P,Huttner W B

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference44 articles.

1. Characterization of adenohypophysial polypeptides by two-dimensional gel electrophoresis

2. Characterization of adenohypophysial polypeptides by two-dimensional gel electrophoresis

3. Tyrosine-O-sulfated proteins of PC12 pheochromocytoma cells and their sulfation by a tyrosylprotein sulfotransferase.

4. The major tyrosine-sulfated protein of the bovine anterior pituitary is a secretory protein present in gonadotrophs, thyrotrophs, mammotrophs, and corticotrophs.

5. Secretogranins I and II: two tyrosine-sulfated secretory proteins common to a variety of cells secreting peptides by the regulated pathway.

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