Amino terminal sequence of amyloid P-component isolated from serum

Merrill Benson, Martha Skinner

Research output: Contribution to journalArticle

9 Citations (Scopus)

Abstract

Amyloid AP (protein SAP) has been isolated from human serum by affinity chromatography using specific antiserum and shown to have the same immunologic and ultrastructural characteristics as the pentagonal protein isolated from amyloid tissue (AP). Polyacrylamide gel electrophoresis in SDS reveals a single subunit of 25,000 daltons for both SAP and AP preparations. N-terminal amino acid sequence of this alpha globulin to 13 residues reveals complete homology with the tissue-extracted protein, suggesting that AP is incorporated into, or adsorbed onto, amyloid fibrils without biochemical alteration.

Original languageEnglish
Pages (from-to)78-83
Number of pages6
JournalJournal of Laboratory and Clinical Medicine
Volume92
Issue number1
StatePublished - 1978

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Serum Amyloid P-Component
Amyloidogenic Proteins
Amyloid
Alpha-Globulins
Tissue
Affinity chromatography
Electrophoresis
Affinity Chromatography
Immune Sera
Polyacrylamide Gel Electrophoresis
Amino Acid Sequence
Proteins
Amino Acids
Serum

ASJC Scopus subject areas

  • Medicine(all)
  • Pathology and Forensic Medicine

Cite this

Amino terminal sequence of amyloid P-component isolated from serum. / Benson, Merrill; Skinner, Martha.

In: Journal of Laboratory and Clinical Medicine, Vol. 92, No. 1, 1978, p. 78-83.

Research output: Contribution to journalArticle

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