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Cited by 191

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Molecular basis of beta-galactosidase alpha-complementation.

Open access
Langley, K E, Villarejo, M R, Fowler, A V, Zamenhof, P J, Zabin, I·1975·Proceedings of the National Academy of Sciences

Abstract

In previous studies, a cyanogen bromide peptide derived from amino-acid residues 3-92 of beta-galactosidase (EC 3.2.1.23; beta-D-galactoside galactohydrolase) was shown to have alpha-donor activity in intracistronic alpha-complementation. We have now isolated the defective beta-galactosidase alpha-acceptor protein from the deletion mutant strain M15 of Escherichia coli and find that it lacks residues 11-41 of betal-galactosidase. This is demonstrated by the isolation and sequence determination of a cyanogen bromide peptide from the M15 protein, which is identical to the corresponding peptide from beta-galactosidase except for the missing amino acids. We conclude that the alpha-donor peptide restores the region missing in the M15 protein.

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Metadata

Authors
Langley, K. E., Villarejo, M. R., Fowler, A. V., Zamenhof, P. J., & Zabin, I.
Venue
Proceedings of the National Academy of Sciences
Published
1975-04
Volume
72
Issue
4
Pages
1254-1257
ISSN
  • 0027-8424 (ISSN-L)
  • 1091-6490
OpenAlex
W1975646429
Cited by
191
References
1
FWCI
4.15
Type
journal article
Language
en
Open access
green

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CoChat. (2026). Citation check: Molecular basis of beta-galactosidase alpha-complementation. https://app.cochat.ai/papers/10.1073/pnas.72.4.1254
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Langley, K. E., Villarejo, M. R., Fowler, A. V., Zamenhof, P. J., & Zabin, I. (1975). Molecular basis of beta-galactosidase alpha-complementation. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.72.4.1254

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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.