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Cited by 545

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Identification of a calcium-binding protein as a calcium-dependent regulator of brain adenylate cyclase.

Open access
Brostrom, C O, Huang, Y C, Breckenridge, B M, Wolff, D J·1975·Proceedings of the National Academy of Sciences

Abstract

An activating factor of adenylate cyclase (EC 4.6.1.1) HAS BEEN OBTAINED FROM DETERGENT-DISPERSED PREPARATIONS OF PORCINE CEREBRAL CORTEX BY COLUMN CHROMATOGRAPHY ON ECTEOLA-cellulose. The factor was identified by acrylamide gel electrophoresis and by enzyme activation studies as the Ca2+-binding protein that regulates the activity of a brain cyclic nucleotide phosphodiesterase. This Ca2+-binding protein confers a Ca2+-dependent activation upon the adenylate cyclase, which is reversed by the subsequent addition of egta in excess of the free Ca2+. It is proposed that this Ca2+-dependent regulator controls enzymatic activities responsible for the synthesis of adenosine 3':5'-monophosphate and for the hydrolysis of guanosine 3':5'-monophosphate.

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Metadata

Authors
Brostrom, C. O., Huang, Y. C., Breckenridge, B. M., & Wolff, D. J.
Venue
Proceedings of the National Academy of Sciences
Published
1975-01
Volume
72
Issue
1
Pages
64-68
ISSN
  • 0027-8424 (ISSN-L)
  • 1091-6490
OpenAlex
W2028519419
Cited by
545
References
0
FWCI
18.04
Type
journal article
Language
en
Open access
green

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CoChat. (2026). Citation check: Identification of a calcium-binding protein as a calcium-dependent regulator of brain adenylate cyclase. https://app.cochat.ai/papers/10.1073/pnas.72.1.64
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Brostrom, C. O., Huang, Y. C., Breckenridge, B. M., & Wolff, D. J. (1975). Identification of a calcium-binding protein as a calcium-dependent regulator of brain adenylate cyclase. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.72.1.64

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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.