ISOLATION AND IDENTIFICATION BY SEQUENCE ANALYSIS OF EXPERIMENTALLY INDUCED GUINEA PIG AMYLOID FIBRILS

Amyloidosis was produced experimentally in guinea pigs by multiple casein injections. Amyloid fibrils were isolated and fractionated and a protein obtained that had an amino acid composition comparable with A protein, a unique nonimmunoglobulin constituent of secondary amyloid deposits. N-terminal s...

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Detalles Bibliográficos
Autores principales: Skinner, Martha, Cathcart, Edgar S., Cohen, Alan S., Benson, Merrill D.
Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 1974
Materias:
Brief Definitive Reports
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2139617/
https://www.ncbi.nlm.nih.gov/pubmed/4213201
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author Skinner, Martha
Cathcart, Edgar S.
Cohen, Alan S.
Benson, Merrill D.
author_facet Skinner, Martha
Cathcart, Edgar S.
Cohen, Alan S.
Benson, Merrill D.
author_sort Skinner, Martha
collection PubMed
description Amyloidosis was produced experimentally in guinea pigs by multiple casein injections. Amyloid fibrils were isolated and fractionated and a protein obtained that had an amino acid composition comparable with A protein, a unique nonimmunoglobulin constituent of secondary amyloid deposits. N-terminal sequence analysis demonstrated a sequence homologous with that of A proteins from human and monkey preparations but preceded by a 5-residue peptide which had an N-terminal histidine. A definite species specificity in A protein from human and guinea pig was identified on immunologic analysis.
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spelling pubmed-21396172008-04-17 ISOLATION AND IDENTIFICATION BY SEQUENCE ANALYSIS OF EXPERIMENTALLY INDUCED GUINEA PIG AMYLOID FIBRILS Skinner, Martha Cathcart, Edgar S. Cohen, Alan S. Benson, Merrill D. J Exp Med Brief Definitive Reports Amyloidosis was produced experimentally in guinea pigs by multiple casein injections. Amyloid fibrils were isolated and fractionated and a protein obtained that had an amino acid composition comparable with A protein, a unique nonimmunoglobulin constituent of secondary amyloid deposits. N-terminal sequence analysis demonstrated a sequence homologous with that of A proteins from human and monkey preparations but preceded by a 5-residue peptide which had an N-terminal histidine. A definite species specificity in A protein from human and guinea pig was identified on immunologic analysis. The Rockefeller University Press 1974-09-01 /pmc/articles/PMC2139617/ /pubmed/4213201 Text en Copyright © 1974 by The Rockefeller University Press This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/).
spellingShingle Brief Definitive Reports
Skinner, Martha
Cathcart, Edgar S.
Cohen, Alan S.
Benson, Merrill D.
ISOLATION AND IDENTIFICATION BY SEQUENCE ANALYSIS OF EXPERIMENTALLY INDUCED GUINEA PIG AMYLOID FIBRILS
title ISOLATION AND IDENTIFICATION BY SEQUENCE ANALYSIS OF EXPERIMENTALLY INDUCED GUINEA PIG AMYLOID FIBRILS
title_full ISOLATION AND IDENTIFICATION BY SEQUENCE ANALYSIS OF EXPERIMENTALLY INDUCED GUINEA PIG AMYLOID FIBRILS
title_fullStr ISOLATION AND IDENTIFICATION BY SEQUENCE ANALYSIS OF EXPERIMENTALLY INDUCED GUINEA PIG AMYLOID FIBRILS
title_full_unstemmed ISOLATION AND IDENTIFICATION BY SEQUENCE ANALYSIS OF EXPERIMENTALLY INDUCED GUINEA PIG AMYLOID FIBRILS
title_short ISOLATION AND IDENTIFICATION BY SEQUENCE ANALYSIS OF EXPERIMENTALLY INDUCED GUINEA PIG AMYLOID FIBRILS
title_sort isolation and identification by sequence analysis of experimentally induced guinea pig amyloid fibrils
topic Brief Definitive Reports
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2139617/
https://www.ncbi.nlm.nih.gov/pubmed/4213201
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AT cohenalans isolationandidentificationbysequenceanalysisofexperimentallyinducedguineapigamyloidfibrils
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