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Speaker 0 describes an ICP analysis (Inductively Coupled Plasma Mass Spectrometry) of white clots, initially encountered about three years ago from samples provided by Richard. Mike Adams presented the initial findings. The ICP analysis showed the highest element in the white clots was phosphorus, followed by sodium, tin, then sulfur and carbon. They also found that there were no normal blood marker elements present in the white clots. Two laboratories in Europe were used to replicate the results; both reported aberrantly high levels of phosphorus, tin, sulfur, sodium, and carbon.
To investigate further, they performed High Performance Liquid Chromatography (HPLC) to identify protein components. The highest level of protein found was fibrinogen. The HPLC analysis determined the kinds of fibrinogen chains present, and it showed that in the white clots the beta chain far exceeded the alpha and gamma chains, with a beta-gamma-alpha ratio. They noted they were not biochemists or medically qualified, but conducted simple research to understand why fibrinogen content was so high. Fibrinogen forms fibrils, which aligns with John O’Learny’s description of white clots as calamari-like in texture, matching the expected texture from fibrin.
An amino acid analysis by colleagues revealed high levels of proline, aspartic acid, lysine, and about 18 other amino acids, all with phosphorus affinity. They reiterate that the element with the highest confirmed concentration in the white clot is phosphorus. They state that aberrant phosphorylation pathways can cause a range of problems in the human body.
They claim three separate pieces of analysis confirm their findings, allowing them to piece together the pathway to the formation of white clots. They connect this to injections that use a lipid nanoparticle carrier, specifically a phospholipid. Their analysis indicates that when the phospholipid releases the mRNA core of the lipid nanoparticle, it exposes a phosphorus head of the phospholipid. The phospholipid reacts within the bloodstream with naturally formed fibrinogen, nucleating the white clot formation. They claim over 200 peer-reviewed papers confirm the pathway described.
They specify that the DSPC phospholipid encapsulating the lipid nanoparticle liberates 80 to 90% of raw phosphorus heads as it releases the mRNA core. Those phosphorus heads react with fibrinogen in the bloodstream, causing the sandy blood and coffee-ground appearance as the nucleation pathway to final white clot formation. They add that the spike protein binds to phosphorylated fibrinogen; the body generates methylcetiopridine-generated spike protein in the bloodstream, which coagulates with phosphorylated fibrinogen, feeding a monomeric reaction that continues to grow. These particles are free-flowing in the blood and find anchor points on damaged endothelial layers. When endothelial layers are damaged via inflammation and the cytokine storm induced by the spike protein, the natural phospholipid layer of the endothelium opens up and forms anchor points for these nuclei. From these anchor points, the clots begin to grow. They acknowledge the complexity but describe this as a simple encapsulation of the process.