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Familial amyloidosis in different kindreds is associated with a variety of point mutations in the prealbumin gene, resulting in prealbumin variants which are believed to be amyloidogenic, i.e. prone to form amyloid fibrils. In the most common amyloid-associated variant, there is a methionine for valine substitution in position 30. We have studied the prealbumin-derived amyloid protein ASc1 in the common age-related senile systemic amyloidosis. Evidence is presented that there is no abnormality in the primary structure of prealbumin in this disease and that, in addition to complete prealbumin, fibrils contain prealbumin fragments lacking a significant part of the N-terminus.
G G Cornwell, and
K Sletten, and
B Johansson, and
P Westermark
November 1995,
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G G Cornwell, and
K Sletten, and
B Johansson, and
P Westermark
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G G Cornwell, and
K Sletten, and
B Johansson, and
P Westermark
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G G Cornwell, and
K Sletten, and
B Johansson, and
P Westermark
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G G Cornwell, and
K Sletten, and
B Johansson, and
P Westermark
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G G Cornwell, and
K Sletten, and
B Johansson, and
P Westermark
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G G Cornwell, and
K Sletten, and
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P Westermark
January 1980,
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G G Cornwell, and
K Sletten, and
B Johansson, and
P Westermark
February 2021,
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G G Cornwell, and
K Sletten, and
B Johansson, and
P Westermark
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G G Cornwell, and
K Sletten, and
B Johansson, and
P Westermark
September 1978,
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