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Complete Primary Structure of Protein Phosphatase Inhibitor‐1 from Rabbit Skeletal Muscle

AITKEN, Alastair, BILHAM, Terry, COHEN, Philip·1982·European Journal of Biochemistry

Abstract

The complete primary structure of protein phosphatase inhibitor‐1 has been determined. The protein consists of a single polypeptide chain of 165 residues, molecular weight 18640. The threonine residue that must be phosphorylated for activation is at position 35 and the active cyanogen bromide peptide, CB‐1, comprises residues 2–66. The N‐terminal methionine is acetylated and 40% of the inhibitor‐1 molecules lack the C‐terminal dipeptide Ala‐Val. Serine‐67 is substantially phosphorylated in vivo, but this phosphoserine residue does not appear to influence the activity of inhibitor‐1.

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Metadata

Authors
AITKEN, A., BILHAM, T., & COHEN, P.
Venue
European Journal of Biochemistry
Publisher
Wiley
Published
1982-08
Volume
126
Issue
2
Pages
235-246
ISSN
  • 0014-2956 (ISSN-L)
  • 1432-1033
OpenAlex
W2025925528
Cited by
163
References
0
FWCI
5.57
Type
journal article
Language
en
Open access
closed

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CoChat. (2026). Citation check: Complete Primary Structure of Protein Phosphatase Inhibitor‐1 from Rabbit Skeletal Muscle. https://app.cochat.ai/papers/10.1111/j.1432-1033.1982.tb06771.x
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AITKEN, A., BILHAM, T., & COHEN, P. (1982). Complete Primary Structure of Protein Phosphatase Inhibitor‐1 from Rabbit Skeletal Muscle. European Journal of Biochemistry. https://doi.org/10.1111/j.1432-1033.1982.tb06771.x

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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.