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Cited by 349

The DOI matches its Crossref record; 24 of the 24 references it cites were found in a registry or an index.

Myoplasmic binding of fura-2 investigated by steady-state fluorescence and absorbance measurements

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Konishi, M., Olson, A., Hollingworth, S., Baylor, S.M.·1988·Biophysical Journal

Abstract

Binding of the fluorescent Ca2+ indicator dye fura-2 by intracellular constituents has been investigated by steady-state optical measurements. Fura-2's (a) fluorescence intensity, (b) fluorescence emission anisotropy, (c) fluorescence emission spectrum, and (d) absorbance spectra were measured in glass capillary tubes containing solutions of purified myoplasmic proteins; properties b and c were also measured in frog skeletal muscle fibers microinjected with fura-2. The results indicate that more than half, and possibly as much as 85%, of fura-2 molecules in myoplasm are in a protein-bound form, and that the binding changes many properties of the dye. For example, in vitro characterization of the Ca2+-dye reaction indicates that when fura-2 is bound to aldolase (a large and abundant myoplasmic protein), the dissociation constant of the dye for Ca2+ is three- to fourfold larger than that measured in the absence of protein. The problems raised by intracellular binding of fura-2 to cytoplasmic proteins may well apply to cells other than skeletal muscle fibers.

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Metadata

Authors
Konishi, M., Olson, A., Hollingworth, S., & Baylor, S. M.
Venue
Biophysical Journal
Publisher
Elsevier BV
Published
1988-12
Volume
54
Issue
6
Pages
1089-1104
ISSN
0006-3495 (ISSN-L)
OpenAlex
W1999132987
Cited by
349
References
24
FWCI
27.38
Type
journal article
Language
en
Open access
hybrid

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CoChat. (2026). Citation check: Myoplasmic binding of fura-2 investigated by steady-state fluorescence and absorbance measurements. https://app.cochat.ai/papers/10.1016/s0006-3495(88)83045-5
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Konishi, M., Olson, A., Hollingworth, S., & Baylor, S. M. (1988). Myoplasmic binding of fura-2 investigated by steady-state fluorescence and absorbance measurements. Biophysical Journal. https://doi.org/10.1016/s0006-3495(88)83045-5

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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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