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Two-dimensional gel analysis of soluble proteins. Characterization of guinea pig exocrine pancreatic proteins.

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Scheele, G A·1975·Journal of Biological Chemistry

Abstract

A two-dimensional gel technique using slab gel isoelectric focusing in the first dimension and sodium dodecyl sulfate gradient gel electrophoresis in the second dimension has been developed for the separation of soluble proteins larger than 10,000 daltons. The technique is sensitive to 0.6 mug of protein and recovery of radiolabeled proteins averages 90%. Analysis of secretory protein from the guinea pig exocrine pancreas shows the presence of 19 distinct high molecular weight proteins. Each of these proteins has been characterized by isoelectric point, molecular weight, and proportionate mass. Thirteen of the 19 proteins have been identified by actual or potential enzymatic activity,accounting for 96% of the protein mass resolved by the two-dimensional gels.

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Metadata

Authors
Scheele, G. A.
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
1975-07
Volume
250
Issue
14
Pages
5375-5385
ISSN
0021-9258 (ISSN-L)
OpenAlex
W1550351158
Cited by
391
References
0
FWCI
7.36
Type
journal article
Language
en
Open access
hybrid

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CoChat. (2026). Citation check: Two-dimensional gel analysis of soluble proteins. Characterization of guinea pig exocrine pancreatic proteins. https://app.cochat.ai/papers/10.1016/s0021-9258(19)41192-7
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Scheele, G. A. (1975). Two-dimensional gel analysis of soluble proteins. Characterization of guinea pig exocrine pancreatic proteins. Journal of Biological Chemistry. https://doi.org/10.1016/s0021-9258(19)41192-7

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.