Calcium binding to spinach (Spinacia oleracea L.) stromal proteins was examined by dual-wavelength spectrophotometry using the metallochromic indicator tetramethylmurexide. The data are consistent with the existence of at least two, probably independent, classes of binding sites. The total number of
Spinach ferredoxin is a calcium-binding protein
β Scribed by Barbara Surek; Georg Kreimer; Michael Melkonian; Erwin Latzko
- Book ID
- 104752989
- Publisher
- Springer-Verlag
- Year
- 1987
- Tongue
- English
- Weight
- 455 KB
- Volume
- 171
- Category
- Article
- ISSN
- 0032-0935
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β¦ Synopsis
Spinach-leaf ferredoxin was identified as a calcium-binding protein by (45)Ca autoradiography on nitrocellulose membranes and with the cationic carbocyanine dye 1-ethyl-2-[3-(1-ethylnaphtho[1,2-d]thiazolin-2-ylidene)-2-methylpropenyl] naphtho[1,2-d]thiazolium bromide ("stains-all"). Binding of (45)Ca was observed at pH 6.8 and pH 7.8 and in the presence of 5 mM and 20 mM MgCl2. At the higher MgCl2 concentration the Ca(2+)-binding capacity is reduced. Only micromolar concentrations of LaCl3, however, are required to achieve a similar effect. Both the oxidized and reduced forms of ferredoxin bind calcium.
π SIMILAR VOLUMES
## Abstract We have purified a prominent 110βkDa protein (p110) from 1.6 M NaCl extracts of rat liver nuclei that appears to bind Ca^2+^. p110 was originally identified by prominent blue staining with βStainsβAllβ in sodium dodecyl sulfateβpolyacrylamide gels and was observed to specifically bind r
Previously, a ferredoxin-type iron-sulfur protein, frx B protein, was identified in a high-salt extract of the purified thylakoid membrane of Chlamydomonas reinhardtii, a unicellular green alga. Polyclonal antibody was raised against a synthetic pentadecameric peptide with an amino acid sequence cor