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Updated: May 11, 2026

Rapid Generation of Amyloid from Native Proteins In vitro
Published on: December 6, 2013
Beta-2 microglobulin is an amyloidogenic protein in man
Abstract:
Curvilinear fibrils with the tinctorial properties of amyloid were isolated from a patient with bone and joint involvement complicating chronic dialysis for renal disease. Subunit fractions of 24,000 and 12,000 mol wt were identified after gel filtration under dissociating conditions, the latter containing a significant amount of a dimer of the former. This was confirmed by Edman degradation of each fraction, which yielded the amino terminal sequence of normal human beta-2 microglobulin (B2M) to residues 20 and 30, respectively. The size of the subunit protein (12,000 mol wt) and the amino acid composition make it likely that intact B2M is a major constituent of the fibrils. B2M is thus another example of a low molecular weight serum protein, with a prominent beta-pleated sheet structure, that may adopt the fibrillar configuration of amyloid in certain pathologic states.
Insights
Amyloid-like fibrils were found in a patient undergoing dialysis. These fibrils are composed of beta-2 microglobulin (B2M), a serum protein, suggesting B2M can form amyloid structures in disease.
Area of Science:
- Biochemistry
- Pathology
- Nephrology
Background:
- Amyloidosis is characterized by protein misfolding and fibril formation.
- Chronic kidney disease and dialysis are associated with various complications.
Observation:
- Curvilinear amyloid-like fibrils were isolated from a patient with bone and joint issues related to chronic dialysis.
- Gel filtration and Edman degradation were used to analyze the fibril composition.
Findings:
- The fibrils were found to be composed of beta-2 microglobulin (B2M).
- Subunit fractions of 24,000 and 12,000 mol wt were identified, with the smaller fraction containing a dimer.
- Edman degradation confirmed the amino-terminal sequence of B2M in the subunit fractions.
Implications:
- Beta-2 microglobulin (B2M) can form amyloid fibrils in pathological conditions.
- This finding expands the understanding of amyloidosis and its potential triggers.
- Low molecular weight serum proteins with beta-pleated sheet structures may be prone to fibril formation.
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