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PMID: 2422756 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

Pancreatic zymogen granules differ markedly in protein composition.

Science (New York, N.Y.) ·Vol. 232 ·No. 4752 ·1986-05-16 ·Pages 871-3

Mroz EA, Lechene C

Abstract

The activities of both chymotrypsin and amylase in individual zymogen granules of rat pancreas were measured by means of micromanipulation and microfluorometric methods. The enzyme content and the ratio of amylase to chymotrypsin varied widely among granules taken from the same animal. These results are compatible with short-term nonparallel bulk secretion of the two enzymes through exocytosis. The distribution of each enzyme activity in a population of granules suggests quantal packaging of amylase and chymotrypsinogen into the granules.

MeSH Terms
Amylases/analysis Animals Chymotrypsin/analysis Cytoplasmic Granules/analysis Exocytosis Female Pancreas/metabolism Rats Rats, Inbred Strains
Chemicals
Amylases Chymotrypsin
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Mroz E A
Lechene C
Article Info
Journal
Science (New York, N.Y.)
Abbr.
Science
ISSN
0036-8075
Published
1986-05-16
Pages
871-3
Language
English
Region
United States
NLM ID
0404511
Subset
IM
Grants
NIADDK NIH HHS · AM26488 · United States
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