HUMAN AMYLOID PROTEIN: CHEMICAL VARIABILITY AND HOMOGENEITY

M. HARADA ¹, C. ISERSKY ¹, P. CUATRECASAS ¹, D. PAGE ¹, H. A. BLADEN ¹, E. D. EANES ¹, H. R. KEISER ¹, and G. G. GLENNER ¹

¹ Laboratory of Experimental Pathology, National Institute of Arthritis and Metabolic Diseases, National Institutes of Health, Bethesda, Maryland 20014

The morphology of the fibril of amyloid derived from different individuals is similar, but occasionally significant differences are noted. All human amyloid filaments have a "-pleated sheet" conformation as revealed by x-ray diffraction, and those examined after orientation show a "cross-" pattern. All amyloid fibril concentrates studied so far can be fractionated to obtain the major amyloid protein component(s) by sequential gel filtration with 5 M guanidine-HCl in 1 N acetic acid on Sepharose 4B and Sephadex G-100 or G-75 columns with the removal of over 28% of proteins representing minor constituents. The major amyloid protein(s) obtained from the spleen and/or liver of six patients is found to contain tryptophan, to be deficient in hydroxylysine and hydroxyproline and usually at least one commonly occurring amino acid and to have a high content of dicarboxylic acid and short chain amino acids and unreactive (blocked) NH₂-terminal groups or aspartic acid-asparagine (Asx). However, the amyloid protein(s) from each individual differs from that of the others in molecular weight, in amino acid composition and in the presence or absence of specific tryptic peptides. Amyloid protein(s) from the liver and spleen of the same individual is identical. No chemical characteristics distinguish amyloid proteins derived from cases classified clinically as "primary" from those classified as "secondary." There is a striking chemical similarity between amyloid proteins and the NH₂-terminal variable fragment of the light and heavy chain of immumoglobulin proteins.

CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this?

This article has been cited by other articles:

				H J Lachmann and P N Hawkins Amyloidosis and the lung Chronic Respiratory Disease, November 1, 2006; 3(4): 203 - 214. [Abstract] [PDF]

				M. von Bergen, S. Barghorn, L. Li, A. Marx, J. Biernat, E.-M. Mandelkow, and E. Mandelkow Mutations of Tau Protein in Frontotemporal Dementia Promote Aggregation of Paired Helical Filaments by Enhancing Local beta -Structure J. Biol. Chem., December 14, 2001; 276(51): 48165 - 48174. [Abstract] [Full Text] [PDF]

				G. G. Glenner, D. Ein, E. D. Eanes, H. A. Bladen, W. Terry, and D. L. Page Creation of "Amyloid" Fibrils from Bence Jones Proteins in vitro Science, November 12, 1971; 174(4010): 712 - 714. [Abstract] [PDF]

Guidelines | Subscriptions | About | exPRESS - Current - Archive | Business Information | Contact

The Journal of Histochemistry & Cytochemistry is owned, published, and licensed by The Histochemical Society © 1971