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In the endoplasmic reticulum of beta cells the proinsulin molecule is cleaved in two places, yielding the A and B chains of insulin and an intervening, biologically inactive C peptide.
When the DNAzyme molecule is cleaved by the target, L-histidine, a partial substrate strand is produced, which in turn can hybridize with the capture probe, forming a DNA duplex.
Upon arrival in the MIIC, the Ii molecule is cleaved through the action of proteases leaving a peptide fragment termed CLIP in the MHCII peptide-binding groove [2].
Here, the molecule is cleaved by the sequential actions of beta site APP cleaving enzyme 1 (BACE 1) and the γ-secretase complex to produce a soluble N-terminal fragment (sAPPβ) and a 37 49 amino acid amyloid β-peptide (Aβ) – the so-called 'amylogenic pathway' [4].
Copeptin, the stable C-terminal part of the AVP precursor molecule, is cleaved from pro-AVP during processing and is secreted in an equimolar concentration with AVP.
In one version, the assay measures the amount of thrombin generated over time in platelet poor or platelet rich plasma by monitoring the change in flourescence as a fluorogenic substrate molecule is cleaved by thrombin.
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The majority of BG molecule was cleaved within 2.5 min.
It shows that BG molecule was cleaved into 12 fragments.
It was believed that the first SAM molecule was cleaved to generate a dAdo, which carried out an H-atom abstraction at C2 of the adenosine substrate generating a substrate radical that was methylated by the second SAM molecule.
Many rRNA molecules are cleaved from much larger transcripts and may also be methylated or enzymatically modified.
The organic molecules are cleaved into small carbon species and further transform to amorphous carbon.
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Justyna Jupowicz-Kozak
CEO of Professional Science Editing for Scientists @ prosciediting.com