Amino terminal sequence of amyloid P-component isolated from serum

Merrill D. Benson, Martha Skinner

Research output: Contribution to journalArticle

9 Scopus citations

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 (US)
Pages (from-to)78-83
Number of pages6
JournalThe Journal of Laboratory and Clinical Medicine
Volume92
Issue number1
StatePublished - Jul 1978

ASJC Scopus subject areas

  • Pathology and Forensic Medicine

Fingerprint Dive into the research topics of 'Amino terminal sequence of amyloid P-component isolated from serum'. Together they form a unique fingerprint.

  • Cite this