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Cited by 567

The DOI matches its Crossref record; 16 of the 16 references it cites were found in a registry or an index.

Isolation of a Calcium-Sequestering Protein from Sarcoplasmic Reticulum

Open access
MacLennan, David H., Wong, P. T. S.·1971·Proceedings of the National Academy of Sciences

Abstract

An acidic protein has been extracted from sarcoplasmic reticulum with KCl and deoxycholate. The protein, which remains soluble after extraction, has been highly purified by fractionation on DEAE-cellulose, Sephadex, and hydroxylaptite. It has a molecular weight of 44,000 and contains 392 amino acid residues per molecule, of which 146 are either glutamic or aspartic acid. No phosphorus, sialic acid, or lipid has been detected in the preparation. The protein has been shown to bind up to 970 nmol of Ca ++ per mg (43 mol/mol) at pH 7.5, with an apparent dissociation constant of 4 × 10 -5 M. Preliminary data indicate that the protein is unique to sarcoplasmic reticulum and that it is hydrophobically bonded on the interior of these vesicles. The protein is believed to play a role in sequestering calcium within sarcoplasmic reticulum. The name Calsequestrin is suggested for the protein.

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Metadata

Authors
MacLennan, D. H., & Wong, P. T. S.
Venue
Proceedings of the National Academy of Sciences
Published
1971-06
Volume
68
Issue
6
Pages
1231-1235
ISSN
  • 0027-8424 (ISSN-L)
  • 1091-6490
OpenAlex
W2007709380
Cited by
567
References
16
FWCI
9.23
Type
journal article
Language
en
Open access
green

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CoChat. (2026). Citation check: Isolation of a Calcium-Sequestering Protein from Sarcoplasmic Reticulum. https://app.cochat.ai/papers/10.1073/pnas.68.6.1231
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MacLennan, D. H., & Wong, P. T. S. (1971). Isolation of a Calcium-Sequestering Protein from Sarcoplasmic Reticulum. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.68.6.1231

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

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