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  • 1
    Electronic Resource
    Electronic Resource
    An Unusually Large (83 Amino Acid Residues) Amyloid Fibril Protein AA from a Patient with Waldenström's Macroglobulinaemia and Amyloidosis (1980)
    Oxford, UK : Blackwell Publishing Ltd
    Scandinavian journal of immunology 11 (1980), S. 0 
    Details
    ISSN: 1365-3083
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: The amino acid sequence studies of a human amyloid fibril protein AA derived from a patient with Waldenström's macroglobulinaemia revealed 83 residues. This protein AA was larger than but otherwise very similar to other human AA proteins studied by complete sequencing. Two amino acids were found both in position 52 (Val/Ala) and in position 53 (Trp/Arg), strongly suggesting a polymorphism of AA proteins. Immunologic studies showed the antigenic determinant(s) reacting with antiprotein AA to be located between positions 25 and 76 of the third cyanogen bromide cleavage fragment of the protein.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-3083.1980.tb00023.x
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  • 2
    Electronic Resource
    Electronic Resource
    Oligoclonal Macroglobulinaemia (1972)
    Oxford, UK : Blackwell Publishing Ltd
    Scandinavian journal of immunology 1 (1972), S. 0 
    Details
    ISSN: 1365-3083
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Ninety macroglobulinaemia sera were tested for occurrence of multiple mono clonal immunoglobulins. Thirteen (14%) of the sera contained more than one monoclonal immunoglobulin. The homogeneous macroglobulins were isolated from 3 sera; in each case individually specific antigenic determinants common to the two components were demonstrated, in addition to determinants unique for each component. NH2-terminal amino acid sequence studies in two pa tients showed that the IgM heterogeneity was due to differences in the primary structure of the variable parts of the x (case To) and the μ (case Nae) chains. Macroglobulinaemia appears to be a unique source of homogeneous immuno-globulins from related clones.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-3083.1972.00019.pp.x
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  • 3
    Electronic Resource
    Electronic Resource
    Oligoclonal Macroglobulinaemia (1972)
    Oxford, UK : Blackwell Publishing Ltd
    Scandinavian journal of immunology 1 (1972), S. 0 
    Details
    ISSN: 1365-3083
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Ninety macroglobulinaemia sera were tested for occurrence of multiple monoclonal immunoglobulins. Thirteen (14%) of the sera contained more than one monoclonal immunoglobulin. The homogeneous macroglobulins were isolated from 3 sera; in each case individually specific antigenic determinants common to the two components were demonstrated, in addition to determinants unique for each component. NH2-terminal amino acid sequence studies in two patients showed that the IgM heterogeneity was due to differences in the primary structure of the variable parts of the μ (case Tö) and the μ (case æ) chains. Macroglobulinaemia appears to be a unique source of homogeneous immunoglobulins from related clones.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-3083.1972.tb03731.x
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  • 4
    Electronic Resource
    Electronic Resource
    An Experimental Model in Mink for Studying the Relation Between Amyloid Fibril Protein AA and the Related Serum Protein, SAA (1975)
    Oxford, UK : Blackwell Publishing Ltd
    Scandinavian journal of immunology 4 (1975), S. 0 
    Details
    ISSN: 1365-3083
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Experimental amyloidosis was induced in mink by repeated injections with endotoxin. Amyloid fibrils extracted from liver and spleen were fractionated by gel filtration after treatment with guanidine-hydrochloride and a reducing agent, dithiothreitol. An elution profile very similar to that of human amyloid fibrils, having protein AA as a major component, was obtained. The mink amyloid protein eluted at a position similar to that of human protein AA was by amino acid composition and partial sequence studies shown to be very similar to the latter protein and was called mink protein AA. In addition, a protein AA-related component (protein SAA) was found in increased amounts in serum of amyloidotic mink, providing further evidence of the homology with human amyloidosis. Experimental amyloidosis in mink represents a suitable model for studying amyloid proteins and related serum components.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-3083.1975.tb03721.x
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  • 5
    Electronic Resource
    Electronic Resource
    Tumour-Like Localized Amyloid of the Brain is derived from Immunoglobulin Light Chain (1993)
    Oxford, UK : Blackwell Publishing Ltd
    Scandinavian journal of immunology 37 (1993), S. 0 
    Details
    ISSN: 1365-3083
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: A patient is presented in whom the amyloid component of an intracerebral‘amyloidoma’has been purified and characterized by amino acid sequence analysis. The material originated from an autopsy of a 76-year-old man who 15 years earlier had been operated for an intracerebral‘amyloid tumour'. The tumour had recurred and grown to an almost walnut-sized mass in the right cerebral hemisphere. It was located in the parietal lobe close to the lateral ventricle and had a close connection to the choroid plexus. Histological examination showed large masses of amyloid surrounded by some plasma cells and a few macrophages of the foreign body type, Amino acid sequence analysis of a major fibril subunit protein showed homology with the variable region of a monoclonal lambda immunoglobulin light chain, subgroup III or IV. This shows that the amyloid in the ‘tumour’ was of AL type and presumably derived from local synthesis by plasma cells.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-3083.1993.tb01673.x
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  • 6
    Electronic Resource
    Electronic Resource
    The Revised Amino Acid Sequence of Serum Amyloid A (SAA) Protein in Mink (1993)
    Oxford, UK : Blackwell Publishing Ltd
    Scandinavian journal of immunology 37 (1993), S. 0 
    Details
    ISSN: 1365-3083
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: The revised amino acid sequence of mink protein SAA was shown to be composed of III amino acid residues. The protein has an insertion of eight amino acid residues compared with that reported earlier. Microheterogeneities were observed in positions 6, 10, 24, 27, 67 and 71. The amino acid sequence is in accordance with the SAA mink cDNA sequences, except for the phenylalanine in position 6. The data indicate a third SAA gene in mink.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-3083.1993.tb01686.x
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  • 7
    Electronic Resource
    Electronic Resource
    The Amino Acid Sequence of Serum Amyloid A (SAA) Protein in Mink (1987)
    Oxford, UK : Blackwell Publishing Ltd
    Scandinavian journal of immunology 26 (1987), S. 0 
    Details
    ISSN: 1365-3083
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: The amino acid sequence of serum amyloid A (SAA) protein from mink was established by characterization of peptides derived from digestion of the protein with trypsin and from cleavage with BNPS-skatole. In three positions, two amino acid residues were found, showing that the protein is polymorphic, tn position 10 both valine and isoleucine were found, while only valine was observed in protein AA. Prominent sequence homologies with protein SAA and protein AA from other species were seen, particularly corresponding to the segment between positions 31 and 54, but also in the C-terminal part of protein SAA, which is not shared by protein AA.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-3083.1987.tb02314.x
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  • 8
    Electronic Resource
    Electronic Resource
    Characterization of Amyloid Protein AA and Its Serum Precursor SAA in the Horse (1986)
    Oxford, UK : Blackwell Publishing Ltd
    Scandinavian journal of immunology 23 (1986), S. 0 
    Details
    ISSN: 1365-3083
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Amyloid was extracted from the liver of a horse that had developed amyloidosis after being used for several years for the production of antibodies to bacterial antigens. The amyloid fibrils were shown to he of the AA type. Two AA proteins with molecular weights of 9000 and 11,000 and with identical partial N-terminal amino acid sequences were identified. Marked structural homology with AA from other species including man was seen, although clear species-related antigenic specificity was observed. SAA isolated from an acute phase (septic abortion) horse serum was identical to AA with respect to antigenicity and the 10 first N-terminal amino acid residues that have been studied up to now. The hulk of SAA was present in the high-density lipoprotein complex in serum. Also SAA was heterogeneous with respect to size, most molecules having a molecular weight of 11,000, and a minority 9000.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-3083.1986.tb02007.x
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  • 9
    Electronic Resource
    Electronic Resource
    Antigenic and Chemical Characterization of Non-Immunoglobulin Amyloid Proteins (1972)
    Oxford, UK : Blackwell Publishing Ltd
    Scandinavian journal of immunology 1 (1972), S. 0 
    Details
    ISSN: 1365-3083
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: The results of antigenic and chemical studies on subcomponents of amyloid fibrils secondary to chronic inflammatory diseases are reported. Treatment of amyloid with either guanidine and dithiothreitol or sodium hydroxide followed by gel filtration on Sephadex G-100 revealed two major protein components, one eluted in the void volume (m. w. 〉200, 000), the other having an m. w. of 5, 000. Results from amino acid composition and N-terminal sequences and also antigenic analysis suggest that the components are two different proteins not related to immunoglobulins.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-3083.1972.tb03305.x
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  • 10
    Electronic Resource
    Electronic Resource
    Further Structural and Antigenic Studies of Light-chain Amyloid Proteins (1981)
    Oxford, UK : Blackwell Publishing Ltd
    Scandinavian journal of immunology 14 (1981), S. 0 
    Details
    ISSN: 1365-3083
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: The major subunit protein of amyloid fibrils (758) isolated from a patient with systemic amyloidosis and studied by N-terminal amino acid sequence analysis was found to be almost identical to the sequence of a VλIV Bence-Jones protein and a previously described AλIV amyloid protein. The two AλIV amyloid proteins showed strong antigenic cross-reaction, appearing as antigenic identity in double immunodiffusion tests using anti-AλlV antiserum raised against one or the other of the two proteins. In addition, another new AλV amyloid fibril protein (R.S.) showed strong amino acid sequence homology and antigenic identity in double immunodiffusions with the prototype of the AλV subgroup (the AR protein). Finally, 20 primary or myeloma-associated amyloid proteins were characterized using antisera against the AA and several Ig light-chain-derived amyloid proteins.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-3083.1981.tb00187.x
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