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Science 16 May 1986:
Vol. 232. no. 4752, pp. 871 - 873
DOI: 10.1126/science.2422756
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Articles

Science, Vol 232, Issue 4752, 871-873
Copyright © 1986 by American Association for the Advancement of Science

articles

Pancreatic zymogen granules differ markedly in protein composition

EA Mroz and C Lechene

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.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Identification of a Transferable Sorting Domain for the Regulated Pathway in the Prohormone Convertase PC2.
J. W.M. Creemers, E. F. Usac, N. A. Bright, J.-W. Van de Loo, E. Jansen, W. J.M. Van de Ven, and J. C. Hutton (1996)
J. Biol. Chem. 271, 25284-25291
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Science. ISSN 0036-8075 (print), 1095-9203 (online)