Related Experiment Video

Updated: Aug 15, 2026

Optical Mapping of Intra-Sarcoplasmic Reticulum Ca2+ and Transmembrane Potential in the Langendorff-perfused Rabbit Heart
09:26

Optical Mapping of Intra-Sarcoplasmic Reticulum Ca2+ and Transmembrane Potential in the Langendorff-perfused Rabbit Heart

Published on: September 10, 2015

[Catalytic properties of protein kinase system from rabbit myocardial sarcolemma]

M D Kurskiĭ, Z D Vorobets, S N Marchenko

    Ukrainskii Biokhimicheskii Zhurnal (1978)
    |March 1, 1983
    PubMed

    More Related Videos

    Assaying Protein Kinase Activity with Radiolabeled ATP08:05

    Assaying Protein Kinase Activity with Radiolabeled ATP

    Published on: May 26, 2017

    Purification of the Sarco-Endoplasmic Reticulum Ca2+-ATPase from Rabbit Muscle08:37

    Purification of the Sarco-Endoplasmic Reticulum Ca2+-ATPase from Rabbit Muscle

    Published on: March 21, 2025

    Related Concept Videos

    MAPK Signaling Cascades01:07

    MAPK Signaling Cascades

    Mitogen-activated protein kinase, or MAPK pathway, activates three sequential kinases to regulate cellular responses such as proliferation, differentiation, survival, and apoptosis. The canonical MAPK pathway starts with a mitogen or growth factor binding to an RTK. The activated RTKs stimulate Ras, which recruits Raf or MAP3 Kinase (MAPKKK), the first kinase of the MAPK signaling cascade. Raf further phosphorylates and activates MEK or MAP2 Kinases (MAPKK), which in turn phosphorylates MAP...
    cAMP-dependent Protein Kinase Pathways01:25

    cAMP-dependent Protein Kinase Pathways

    Cyclic Adenosine Monophosphate (cAMP) is an essential second messenger that activates protein kinase A (PKA) and regulates various biological processes. A single epinephrine molecule binds to GPCR and activates several heterotrimeric G proteins, each stimulating multiple adenylyl cyclase, amplifying the signal, and synthesizing large numbers of cAMP molecules. Small changes in cAMP concentration affect PKA activity. The binding of four cAMP molecules induces a conformational change in PKA,...
    Calmodulin-dependent Signaling01:16

    Calmodulin-dependent Signaling

    Calmodulin (CaM) is a calcium-binding protein in eukaryotes that controls various calcium-regulated cellular processes. It has four calcium-binding sites that bind calcium to form the calcium-calmodulin ( Ca2+-CaM) complex. GPCR stimulation increases the calcium levels in the cells that bind to CaM and induces a conformational change.
    The Ca2+-CaM complex does not have enzymatic activity by itself. Instead, the complex binds downstream target proteins, including membrane proteins or enzymes,...
    Transducer Mechanism: Enzyme-Linked Receptors01:27

    Transducer Mechanism: Enzyme-Linked Receptors

    Enzyme-linked receptors are cell-surface receptors acting as an enzyme or associating with an enzyme intracellularly. They make excellent drug targets. Drugs can bind to the extracellular ligand-binding domain or directly affect their enzymatic domain and alter their activity.
    Major types that are helpful drug targets include: