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  2. Calcium in biology - Wikipedia

    en.wikipedia.org/wiki/Calcium_in_biology

    The Ca 2+ concentration of the vacuole may reach millimolar levels. The most striking use of Ca 2+ ions as a structural element in algae occurs in the marine coccolithophores, which use Ca 2+ to form the calcium carbonate plates, with which they are covered. Calcium is needed to form the pectin in the middle lamella of newly formed cells.

  3. Calcium imaging - Wikipedia

    en.wikipedia.org/wiki/Calcium_imaging

    The first real time (video rate) Ca 2+ imaging was carried out in 1986 in cardiac cells using intensified video cameras. [3] Later development of the technique using laser scanning confocal microscopes revealed sub-cellular Ca 2+ signals in the form of Ca 2+ sparks and Ca 2+ blips.

  4. Calcium signaling - Wikipedia

    en.wikipedia.org/wiki/Calcium_signaling

    The Ca 2+ in the myoplasm will diffuse to Ca 2+ regulator sites on the thin filaments. This leads to the actual contraction of the muscle. [15] Contractions of smooth muscle fiber are dependent on how a Ca 2+ influx occurs. When a Ca 2+ influx occurs, cross bridges form between myosin and actin leading to the

  5. Calcium - Wikipedia

    en.wikipedia.org/wiki/Calcium

    In the simplest terms, mountain-building exposes calcium-bearing rocks such as basalt and granodiorite to chemical weathering and releases Ca 2+ into surface water. These ions are transported to the ocean where they react with dissolved CO 2 to form limestone (CaCO 3), which in turn settles to the sea floor where it is incorporated into new rocks.

  6. Calcium pump - Wikipedia

    en.wikipedia.org/wiki/Calcium_pump

    E1⋅2Ca 2+ - cytoplasmic gate open, free Ca 2+ ion exchange occurs between bound ions and those in cytoplasm, closed configuration of N, P, A domains broken, exposing catalytic site E1⋅ ATP - ATP binds and links N to P , P bends, N contacts A , A causes M1 helix to pull up, closes cytoplasmic gate, bound Ca 2+ occluded in transmembrane

  7. Calmodulin - Wikipedia

    en.wikipedia.org/wiki/Calmodulin

    Calmodulin is a small, highly conserved protein that is 148 amino acids long (16.7 kDa). The protein has two approximately symmetrical globular domains (the N- and C- domains) each containing a pair of EF hand motifs [5] separated by a flexible linker region for a total of four Ca 2+ binding sites, two in each globular domain. [6]

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  9. Calcium ATPase - Wikipedia

    en.wikipedia.org/wiki/Calcium_ATPase

    In myocytes (muscle cells) Ca 2+ is normally sequestered (isolated) in a specialized form of endoplasmic reticulum (ER) called sarcoplasmic reticulum (SR). It is a Ca 2+ ATPase that transfers Ca 2+ from the cytosol of the cell to the lumen of the SR at the expense of ATP hydrolysis during muscle relaxation. In the skeletal muscles the calcium ...