Polymorphism of human plasma thyroxine binding prealbumin

Francis E. Dwulet, Merrill Benson

Research output: Contribution to journalArticle

125 Citations (Scopus)

Abstract

Amyloid fibrils from an individual with heredofamilial amyloidosis were found to be composed of plasma prealbumin. To study this protein a three step procedure to isolate prealbumin from plasma was developed. It entailed ion exchange chromatography on DEAE Sephadex, affinity chromatography on Affi-gel Blue and gel filtration on AcA-34. Trypsin Digests of prealbumin were separated by reverse phase HPLC and the pattern compared to that from the normal protein. Only one unexpected peptide was found and it represented the substitution of a methionine for a valine at position 30 in the molecule. This substitution accounts for about 1 3 of the isolated molecules and it represents the first point mutation identified in human plasma prealbumin.

Original languageEnglish
Pages (from-to)657-662
Number of pages6
JournalBiochemical and Biophysical Research Communications
Volume114
Issue number2
DOIs
StatePublished - Jul 29 1983

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Plasma (human)
Prealbumin
Polymorphism
Thyroxine
Cibacron Blue F 3GA
Substitution reactions
Plasmas
Affinity chromatography
DEAE-Dextran
Molecules
Ion Exchange Chromatography
Valine
Amyloidosis
Chromatography
Affinity Chromatography
Point Mutation
Amyloid
Methionine
Trypsin
Gel Chromatography

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

Polymorphism of human plasma thyroxine binding prealbumin. / Dwulet, Francis E.; Benson, Merrill.

In: Biochemical and Biophysical Research Communications, Vol. 114, No. 2, 29.07.1983, p. 657-662.

Research output: Contribution to journalArticle

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