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PMID: 6743341 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Phosphorylation of zymogen granule membrane proteins in intact rat pancreatic acinar cells.

Biochemical and biophysical research communications ·Vol. 122 ·No. 1 ·1984-07-18 ·Pages 413-9

Peiffer A, Gagnon C, Heisler S

Abstract

Phosphorylated substrates of molecular weights 130,000, 70,000, and 29,000, were identified by SDS-gel electrophoresis in zymogen granule membranes of rat pancreatic acinar cells incubated in vitro with protein kinase catalytic subunit. However, when intact cells were incubated with [32P]-orthophosphate, only the 29,000 molecular weight protein was phosphorylated.

MeSH Terms

Animals Catalysis Cytoplasmic Granules/metabolism Enzyme Precursors/metabolism In Vitro Techniques Intracellular Membranes/metabolism Membrane Proteins/metabolism Pancreas/metabolism Phosphoproteins/metabolism Phosphorylation Protein Kinases/metabolism Rats Ribonuclease, Pancreatic Ribosomes/metabolism

Chemicals

Enzyme Precursors Membrane Proteins Phosphoproteins Protein Kinases Ribonuclease, Pancreatic

Authors & Affiliations

3 authors, click to expand affiliations / ORCID

Peiffer A

Gagnon C

Heisler S

Article Info

Journal

Biochemical and biophysical research communications

Abbr.

Biochem Biophys Res Commun

ISSN

0006-291X

DOI

10.1016/0006-291x(84)90491-1

Published

1984-07-18

Pages

413-9

Language

English

Region

United States

NLM ID

0372516

Subset

External Links

PubMed source DOI: 10.1016/0006-291x(84)90491-1 View journal details

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Phosphorylation of zymogen granule membrane proteins in intact rat pancreatic acinar cells.

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