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  • 1
    Electronic Resource
    Electronic Resource
    Familial amyloidotic polyneuropathy: transthyretin (prealbumin) variants in kindreds of Italian origin (1988)
    Springer
    Human genetics 〈Berlin〉 80 (1988), S. 341-343 
    Details
    ISSN: 1432-1203
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary As part of an epidemiological study that aims to characterize chemically the mutation(s) in transthyretin (TTR) related to familial amyloidotic polyneuropathy (FAP) of different ethnic origins, studies were carried out on TTR from two FAP kindreds of Italian origin. Two different criteria were employed in the characterization of TTR from these kindreds: (1) immunoblotting of cyanogen bromide fragments for screening of TTR(Met30) and (2) isoelectric focusing. TTR(Met30) was not detected but other substitutions were demonstrated using isoelectric focusing techniques. One of the variants found is a basic TTR variant. The substitutions occurring in the variant TTRs of these two kindreds are not known and are presently under study.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00273648
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Improved rehydration procedure for polyacrylamide gels in presence of urea: Demonstration of inherited human prealbumin variants by isoelectric focusing in an immobilized pH gradient (1984)
    Weinheim : Wiley-Blackwell
    Electrophoresis 5 (1984), S. 379-381 
    Details
    ISSN: 0173-0835
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Polyacrylamide gels containing immobilized pH gradients (IPGs) are usually extensively washed in deionized water after polymerization and dried when longer storage is required. The original volume of the gel is readjusted by rehydration in water or a solution of appropriate composition and subsequent evaporation, if necessary, by using a fan for weight control. A more convenient procedure is to put the dried gels back into their casting mold used for polymerization and to fill the mold with the appropriate rehydrating solution. Rehydration to the original volume is completed within 30 min for gels of a thickness of 0.5 mm. With gels to be rehydrated in the presence of urea, it was found that water enters the gel matrix faster than urea; consequently, adjustment to the original gel volume at the required urea concentration is not possible in an excess of rehydration solution, but is easily achieved by the modified rehydration procedure. It was also possible to infuse a urea gradient into the gel matrix perpendicular to the pH gradient axis. The effect of urea on the patterns of inherited human prealbumin variants is demonstrated.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.1150050613
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  • 3
    Electronic Resource
    Electronic Resource
    Hybrid isoelectric focusing: Adsorption of proteins onto immobilized pH gradient matrices and desorption by carrier ampholytes (1987)
    Weinheim : Wiley-Blackwell
    Electrophoresis 8 (1987), S. 52-62 
    Details
    ISSN: 0173-0835
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Comparing the separation patterns achieved by hybrid isoelectric focusing in immobilized pH gradients of 1 and 3 meqv/pH/L buffering power, it is demonstrated that a significant proportion of sample protein is lost in gels with the higher buffering power. A buffering power of 1 meqv/pH/L was found to be the lowest acceptable limit for flat bed gel hybrid isoelectric focusing still ensuring adequate control of the immobilized pH gradient. Protein losses were manifested as diminished overall staining intensity, disappearance of individual zones in dilution series, tailing effects and residual material at the application site, all of the above effects being more pronounced for larger than smaller proteins. Adsorption of proteins to charged binding sites of the immobilized pH gradient offers a plausible explanation for the observed phenomena. The visible effects of adsorption could be reduced by the addition of carrier ampholytes, but not by urea or detergents like Triton X-100, 3-(3-chol-amidopropyl)-dimethylammonio-l-propanesulfonate (CHAPS) or octyl β-thio-glucoside, indicating ionic interactions between the immobilized charged groups, carrier ampholytes and proteins. The adsorption phenomena may strongly affect the quantification of proteins in immobilized pH gradients.
    Additional Material: 9 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.1150080111
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  • 4
    Electronic Resource
    Electronic Resource
    Paraffin oil protected high resolution hybrid isoelectric focusing for the demonstration of substitutions of neutral amino acids in denatured proteins: The case of four human transthyretin (prealbumin) variants associated with familial amyloidotic polyneuropathy (1987)
    Weinheim : Wiley-Blackwell
    Electrophoresis 8 (1987), S. 293-297 
    Details
    ISSN: 0173-0835
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: All four sequenced variants of human plasma transthyretin (TTR) with different substitutions of electrically neutral amino acids and associated with familial amyloidotic polyneuropathy (i. e. TTR(Met30), TTR(Ala60), TTR(Tyr77) and TTR(Ser84)) have been separated from the normal TTR monomer by hybrid isoelectric focusing (HIEF) under denaturing conditions. The pI differences from the normal monomer were between 0.0025 and 0.005 pH units corresponding to 0.7-1.4 % of a full charge unit difference. The detectability of these variants by HIEF under denaturing conditions (7 M urea, 50 mM dithiothreitol, 2 % Triton X-100) was explained assuming interaction of the amino acids at the substitution site with a charged amino acid in its close vicinity. It is proposed to distinguish a high from a low level of resolution for HIEF under denaturing conditions to underline the fact that the studied variants could only be detected by extreme flattening of the pH gradient. To provide protection against modification by the laboratory atmosphere the entire gel, including the electrode wicks and sample application site, was covered with a layer of paraffin oil.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.1150080606
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  • 5
    Electronic Resource
    Electronic Resource
    Separation by hybrid isoelectric focusing of normal human plasma transthyretin (prealbumin) and a variant with a methionine for valine substitution associated with familial amyloidotic polyneuropathy (1986)
    Weinheim : Wiley-Blackwell
    Electrophoresis 7 (1986), S. 529-533 
    Details
    ISSN: 0173-0835
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: The human plasma transthyretin (TTR, prealbumin) variant TTR(Met30) has been separated from normal TTR(Val30) by double one-dimensional electrophoresis using polyacrylamide gel electrophoresis followed by hybrid isoelectric focusing. The procedure appears to be appropriate for identification by the screening of patients with familial amyloidotic polyneuropathy of Portuguese type I. This is the second example to support the recently expressed hypothesis (Altland et al., Electrophoresis 1986, 7, 251-259) that substitutions of electrically neutral amino acids (e. g. methionine for valine at position 30) in a polypeptide chain (e. g. the TTR monomer) may be detected by isoelectric focusing under denaturing conditions (e. g. hybrid isoelectric focusing in the presence of 8 M urea, 50 mM dithiothreitol) when the exchange is close to a charged amino acid (e. g. histidine at position 31, pI (TTR) = 5.7, pKa (His) = 6.0).
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.1150071110
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  • 6
    Electronic Resource
    Electronic Resource
    Experimental evidence for flexible slope of immobilized pH gradients poured under computer control (1985)
    Weinheim : Wiley-Blackwell
    Electrophoresis 6 (1985), S. 140-142 
    Details
    ISSN: 0173-0835
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Recently, Altland and Altland (Clin. Chem. 1984, 30, 2098-2103) described three alternative devices for pouring immobilized pH gradients (IPGs) based on simultaneous delivery of a density gradient and a non-density gradient by using high precision burettes under computer control. One of the expected improvements was an unlimited flexibility for the slope of the non-density gradient (e. g. the pH gradient) which is stabilized by the density gradient. The human plasma proteins prealbumin and apolipoprotein AI and some of their inherited variants are demonstrated by double one-dimensional electrophoresis in the sequence polyacrylamide gel electrophoresis followed by isoelectric focusing (IEF) in IPGs of varying slopes in the range of pH 4 to 7. It is shown that the patterns obtained follow the expectations from the gradients drawn on the computer. We conclude that the new devices for pouring IPGs can provide a valuable tool for the easy handling of complex separation problems to be solved by IEF.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.1150060310
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