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Cited by 170

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Synthesis and processing of an Escherichia coli alkaline phosphatase precursor in vitro.

Open access
Inouye, H, Beckwith, J·1977·Proceedings of the National Academy of Sciences
DOI 10.1073/pnas.74.4.1440
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Abstract

Alkaline phosphatase [orthophosphoric-monoester phosphohydrolase (alkaline optimum), EC 3.1.3.1] of E. coli was synthesized in a cell-free system, and the size of the direct translation product was analyzed. The product has a higher molecular weight than the mature alkaline phosphatase found in the periplasm. The direct translation product can be processed to the mature size by an E. coli membrane fraction; the processing activity copurifies with the outer-membrane fraction. The presumed precursor can dimerize to form active enzyme without being processed, and the resultant enzyme appears to be more hydrophobic than the mature enzyme. These findings are discussed in connection with the "signal hypothesis" proposed for the excretion of proteins across membranes.

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Metadata

Authors
Inouye, H., & Beckwith, J.
Venue
Proceedings of the National Academy of Sciences
Publisher
Proceedings of the National Academy of Sciences
Published
1977-04
Volume
74
Issue
4
Pages
1440-1444
ISSN
  • 0027-8424 (ISSN-L)
  • 1091-6490
DOI
10.1073/pnas.74.4.1440
OpenAlex
W2089366909
Cited by
170
References
0
FWCI
22.92
Type
journal article
Language
en
Open access
green

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CoChat. (2026). Citation check: Synthesis and processing of an Escherichia coli alkaline phosphatase precursor in vitro. https://app.cochat.ai/papers/10.1073/pnas.74.4.1440
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Inouye, H., & Beckwith, J. (1977). Synthesis and processing of an Escherichia coli alkaline phosphatase precursor in vitro. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.74.4.1440

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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.