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This increases the pH of the lysosome from 4 to 6.
The lysosome is often called the "waste disposal plant" of the cell.
In the lysosome it is proteolytically processed into its active form.
From here, they are together transported to early and late endosomes until reaching the lysosome.
The last function of a lysosome is to digest the cell itself through autolysis.
The lysosome contains a large number of proteases such as cathepsins.
Moreover, gallium is mostly found as a salt in lysosome within the cell.
Its cell wall prevents the fusion of the phagosome with a lysosome.
This is caused by the acidic conditions which occur inside the host cell's lysosome.
It is localized in the lysosome and has a molecular weight of 59700 Daltons.
The phagosome then combines with a lysosome to create a phagolysosome.
The size of a lysosome varies from 0.1-1.2 μm.
Doa4 removes ubiquitin from cargo proteins being targeted to the lysosome.
Unlike them, cathepsin S remains stable and it has a physiological role outside the lysosome.
Sphingosine is formed via degradation of sphingolipid in the lysosome.
Vesicles can also fuse with other target cell compartments, such as a lysosome.
Most of other lysosomal proteases are trapped inside the lysosome due to a problem with their stability.
Some bacteria prevent the fusion of a phagosome and lysosome, to form the phagolysosome.
The membrane around a lysosome allows the digestive enzymes to work at the 5 pH they require.
Human β-glucuronidase is located in the lysosome.
Endosomes provide an environment for material to be sorted before it reaches the degradative lysosome.
The phagosome of ingested material is then fused with the lysosome, leading to degradation.
They fuse to make a food vacuole which then fuses with a lysosome to add digestive chemicals.
Microautophagy, on the other hand, involves the direct engulfment of cytoplasmic material into the lysosome.
Multivesicular bodies play a large role in the transport of ubiquitinated proteins and receptors to a lysosome.