Structure of Transthyretin Molecules in Amyloid Fibrills from the Vitreous Body in Individuals with the Met30 Mutation View Full Text


Ontology type: schema:Chapter     


Chapter Info

DATE

1991

AUTHORS

J. Wahlquist , C. Thylén , E. Hættner , O. Sandgren , G. Holmgren , E. Lundgren

ABSTRACT

Amyloid fibrils were isolated from the vitreous body from a heterozygous and and a homozygous individual diagnosed as FAP I (transthyretin met-30) by RFLP. On SDS-PAGE the intact TTR monomer (17 kDa) as well as a dimer was seen. The dimer form was more prominent under nonreducing conditions. Two other bands were also found. The larger 14 kDa band was identified by protein sequencing to correspond to amino acids 49-127, possibly cleaved at a putative serine protease site between amino acids 48 and 49 (lys-thr). A smaller fragment containing a cystein group probably represents the 1-48 fragment or parts of it. More... »

PAGES

587-590

Book

TITLE

Amyloid and Amyloidosis 1990

ISBN

978-94-010-5450-8
978-94-011-3284-8

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/978-94-011-3284-8_144

DOI

http://dx.doi.org/10.1007/978-94-011-3284-8_144

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1001929600


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