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  2. Endoplasmic reticulum - Wikipedia

    en.wikipedia.org/wiki/Endoplasmic_reticulum

    It is a type of organelle made up of two subunits – rough endoplasmic reticulum (RER), and smooth endoplasmic reticulum (SER). The endoplasmic reticulum is found in most eukaryotic cells and forms an interconnected network of flattened, membrane-enclosed sacs known as cisternae (in the RER), and tubular structures in the SER.

  3. Microsome - Wikipedia

    en.wikipedia.org/wiki/Microsome

    The study found significant differences between human liver microsomes and human liver S9 fractions in drug-metabolizing enzyme and transporter protein concentrations. The protein-protein correlations of these drug-metabolizing enzymes and transporters was determined relating to the two hepatic preparations.

  4. Hepatocyte - Wikipedia

    en.wikipedia.org/wiki/Hepatocyte

    The typical hepatocyte is cubical with sides of 20-30 μm, (in comparison, a human hair has a diameter of 17 to 180 μm). [1] The typical volume of a hepatocyte is 3.4 x 10 −9 cm 3 . [ 2 ] Smooth endoplasmic reticulum is abundant in hepatocytes, in contrast to most other cell types.

  5. Endoplasmic-reticulum-associated protein degradation

    en.wikipedia.org/wiki/Endoplasmic-reticulum...

    Endoplasmic-reticulum-associated protein degradation is one of several protein degradation pathways in the ER. Endoplasmic-reticulum-associated protein degradation (ERAD) designates a cellular pathway which targets misfolded proteins of the endoplasmic reticulum for ubiquitination and subsequent degradation by a protein-degrading complex, called the proteasome.

  6. Secretion - Wikipedia

    en.wikipedia.org/wiki/Secretion

    Secretion is the movement of material from one point to another, such as a secreted chemical substance from a cell or gland.In contrast, excretion is the removal of certain substances or waste products from a cell or organism.

  7. Chaperone (protein) - Wikipedia

    en.wikipedia.org/wiki/Chaperone_(protein)

    Hsp10/60 (GroEL/GroES complex in E. coli) is the best characterized large (~ 1 MDa) chaperone complex. GroEL (Hsp60) is a double-ring 14mer with a hydrophobic patch at its opening; it is so large it can accommodate native folding of 54-kDa GFP in its lumen. GroES (Hsp10) is a single-ring heptamer that binds to GroEL in the presence of ATP or ADP.

  8. Signal recognition particle - Wikipedia

    en.wikipedia.org/wiki/Signal_recognition_particle

    In eukaryotes, SRP binds to the signal sequence of a newly synthesized peptide as it emerges from the ribosome. [1] This binding leads to the slowing of protein synthesis known as "elongation arrest", a conserved function of SRP that facilitates the coupling of the protein translation and the protein translocation processes. [5]

  9. Lysosome - Wikipedia

    en.wikipedia.org/wiki/Lysosome

    The size of lysosomes varies from 0.1 μm to 1.2 μm. [24] With a pH ranging from ~4.5–5.0, the interior of the lysosomes is acidic compared to the slightly basic cytosol (pH 7.2). The lysosomal membrane protects the cytosol, and therefore the rest of the cell, from the degradative enzymes within the lysosome.

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    difference between ser and rer for class 9 biology notes kpk chapter 1 pdf