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AMYLOID OF HUMAN ISLETS OF LANGERHANS
Author(s) -
Westermark Per
Publication year - 1975
Publication title -
acta pathologica microbiologica scandinavica section c immunology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.909
H-Index - 88
eISSN - 1600-0463
pISSN - 0304-1328
DOI - 10.1111/j.1699-0463.1975.tb01662.x
Subject(s) - islet , amyloid (mycology) , chemistry , medullary carcinoma , fibril , amyloid fibril , amyloidosis , endocrinology , biochemistry , medicine , diabetes mellitus , biology , thyroid , amyloid β , thyroid carcinoma , disease , inorganic chemistry
Islet amyloid concentrates containing a maximum of 50 per cent of amyloid fibrils as estimated by light microscopy were obtained from pancreases of patients with maturity onset diabetes mellitus. When centrifuged, the amyloid did not form a top layer as do most other amyloids, but was found in the bottom layer. This phenomenon and the difficulty in dissolving islet amyloid seemed to be due to inability to separate the amyloid fibrils from each other. In SDS electrophoresis, one or two weak bands corresponding to a molecular weight of about 3000–4000 daltons were observed, but most of the material did not enter the poly‐acrylamide gels. Spectrophotometrically, no tryptophane and almost no tyrosine were demonstrated. It is concluded that the major islet amyloid protein differs fundamentally from other characterized amyloid proteins and, probably together with amyloid of medullary carcinoma of the thyroid, forms a new class of amyloid proteins.