Related Concept Videos
Calmodulin-dependent Signaling
The Ca2+-CaM complex does not have enzymatic activity by itself. Instead, the complex binds downstream target proteins, including membrane proteins or enzymes,...
Skeleton and Calcium Homeostasis
Feedback Regulation of Calcium Concentration
Various transmembrane receptors, such as G protein-coupled receptors (GPCRs), elicit a response to extracellular signals by increasing cytosolic calcium. Activated GPCRs...
Imaging Studies for Cardiovascular System VI: Calcium -Scoring CT
Protein Transport to the Stroma
Protein complexes called the translocon of the outer chloroplast membrane or TOC complex, and the translocon of the inner chloroplast membrane or TIC complex mediate the...
You might also read
Related Articles
Articles linked to this work by shared authors, journal, and citation graph.
Oat leaf phosphoglucose isomerase: competitive inhibition by erythrose-4-phosphate.
Related Experiment Video
Updated: May 6, 2026

Targeting Cysteine Thiols for in Vitro Site-specific Glycosylation of Recombinant Proteins
Published on: October 4, 2017
Calcium binding by spinach stromal proteins.
G Kreimer1, B Surek, I E Woodrow
1Botanisches Institut der Westfälischen Wilhelms-Universität, Schloßgarten 3, D-4400, Münster, Federal Republic of Germany.
Spinach stromal proteins exhibit calcium binding with multiple sites and varying affinities. Changes in pH significantly impact calcium binding, influencing stromal free calcium levels between light and dark conditions.
Area of Science:
- Plant biochemistry
- Photosynthesis research
- Molecular plant physiology
Background:
- Calcium ions (Ca2+) play crucial roles in plant cell signaling and photosynthesis.
- Understanding calcium binding to stromal proteins is essential for elucidating photosynthetic regulation.
- Previous studies have investigated calcium binding in thylakoid membranes, but stromal interactions require further clarification.
Purpose of the Study:
- To quantify calcium binding to spinach stromal proteins.
- To characterize the binding sites and affinities for calcium.
- To investigate the influence of environmental factors (pH, other ions) on calcium binding and its physiological relevance in photosynthesis.
Main Methods:
- Dual-wavelength spectrophotometry utilizing the metallochromic indicator tetramethylmurexide.
- Competitive inhibition assays with magnesium (Mg2+) and lanthanum (La3+) ions.
- Analysis of calcium binding under varying pH conditions and comparison with existing thylakoid data.
Main Results:
- Spinach stromal proteins possess at least two independent classes of calcium binding sites.
- Total binding sites ranged from 90-155 nmol·mg(-1) protein with average binding constants of 1.1-2.7·mM(-1).
- pH decrease (7.8 to 7.1) reduced binding sites but increased average affinity, leading to higher free Ca2+ in the stroma under dark conditions (pH 7.1) compared to light (pH 7.8).
Conclusions:
- Calcium binding to spinach stromal proteins is significant and influenced by pH.
- The study provides evidence for differential free Ca2+ concentrations in the stroma between light and dark conditions.
- These findings suggest a regulatory role for stromal calcium binding in photosynthetic processes.

