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  • 1
    Electronic Resource
    Electronic Resource
    Development of a de novo tumorous necrotic lesion in the liver after transcatheter arterial embolization combined with iodized oil infusion: Report of a case (1996)
    Springer
    Surgery today 26 (1996), S. 49-52 
    Details
    ISSN: 1436-2813
    Keywords: tumorous necrotic lesion ; Lp-TAE ; hepatic infarction
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract We report herein the case of a 69-year-old woman in whom a hepatic tumorous necrotic lesion was discovered following transcatheter arterial embolization combined with iodized oil infusion (Lp-TAE) for a hepatoma. The lesion, which had not been evident prior to the Lp-TAE, was resected and analyzed pathologically. The portal area distribution in the necrotic lesion was the same as that in the surrounding hepatic tissue, suggesting that the lesion was derived from the nonneoplastic hepatic tissue. Moreover, extensive wall thickening and obstruction were observed in the intrahepatic portal vein and hepatic artery. These findings suggest that the lesion was a focus of hepatic infarction triggered by Lp-TAE.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00311992
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  • 2
    Electronic Resource
    Electronic Resource
    Separation and characterization of Arabidopsis thaliana proteins by two-dimensional gel electrophoresis (1995)
    Weinheim : Wiley-Blackwell
    Electrophoresis 16 (1995), S. 423-430 
    Details
    ISSN: 0173-0835
    Keywords: Two-dimensional polyacrylamide gel electrophoresis ; Arabidopsis thaliana ; Gel image analysis ; N-Terminal sequences ; Deblocking by hydrazine vapor ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Arabidopsis (Arabidopsis thaliana) proteins were isolated from five tissues (leaf, stem, root, seed and callus), and separated by two-dimensional gel electrophoresis (2-DE). 2-DE was carried out by immobilized pH gradient (IPG) in the first dimension, and by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) in the second dimension. With the aid of comigrated five-marker proteins, the patterns of 2-DE gels for each tissue were graphically combined by a computer into a single synthetic image for the integrated Arabidopsis protein spots. The protein spot images, altogether 4763, were characterized by both molecular mass and isoelectric point. Partial amino(N)-terminal sequences of 101 protein spots were analyzed by Edman degradation. Fifty seven proteins were partially sequenced and 46 proteins appeared to have blocked N-termini. Deblocking by hydrazine vapor was carried out on 14 proteins and two of them were found to be pyroglutamyl-blocked N-termini. Forty seven new proteins were found by the present investigation.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.1150160169
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  • 3
    Electronic Resource
    Electronic Resource
    Additional possible tools for identification of proteins on one- or two-dimensional electrophoresis (1998)
    Weinheim : Wiley-Blackwell
    Electrophoresis 19 (1998), S. 928-938 
    Details
    ISSN: 0173-0835
    Keywords: Multiple C-terminal sequencing at multisites ; Asp-C cleavage ; Ser/Thr-N cleavage ; Deblocking ; C-terminal sequencing ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Additional, essentially chemical, identification methods of proteins in polyacry-lamide gel electrophoresis are described. Two cleavages of peptide bonds were used at the C-side of aspartic acid with a 0.2% pentafluoropropionic acid (PFPA) aqueous vapor at 90° for 4-16 h, and the N-side of serine/threonine with an S-ethyl trifluorothioacetate vapor at 50° for 6-24 h. The products were analyzed by mass spectrometry- peptide mass fingerprinting. A new type of C-terminal sequencing at multisites of protein was introduced. An aqueous vapor of 90% PFPA at 90° for 2-16 h provided cleavages at the C-side of aspartic acid and the N-side of serine/threonine and simultaneous successive truncation at the C-termini of the cleaved fragments. The product resulted in C-terminal sequences at multisites in proteins by mass spectrometric analysis. The following chemical deblocking methods were used. Anhydrous hydrazine vapor at-5° for 8 h deblocked the N-formyl group, and the vapor at 20° for 4 h deblocked pyrrolidone carboxylate. N-acetylserine/threonine was deblocked by aqueous vapor of 75% PFPA at 50° for 1 h, followed by reaction with p-suifophenylisothiocyanate at pH 6.0. These methods were applied to a variety of protein spots on polyacrylamide gels. A new stepwise C-terminal sequencing of protein from polyacrylamide gels is also described.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.1150190608
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  • 4
    Electronic Resource
    Electronic Resource
    Two-dimensional electrophoresis of plant proteins and standardization of gel patterns (1996)
    Weinheim : Wiley-Blackwell
    Electrophoresis 17 (1996), S. 855-865 
    Details
    ISSN: 0173-0835
    Keywords: Two-dimensional polyacrylamide gel electrophoresis ; Arabidopsis thaliana ; Rice ; Standardization by stripe type markers ; Deblocking with heptafluorobutyric acid vapor ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Proteins of two plants, Arabidopsis thaliana and rice (Oryza sativa) were subjected to two-dimensional electrophoresis analysis with two modifications: (i) comigration of external standard marker proteins with resultant horizontal and vertical stripes in the gel, and (ii) deblocking with a vapor of aqueous heptafluorobutyric acid for N-acetylserine. Approximately 5000 protein spots were separated from both the five tissues of Arabidopsis and the nine tissues of rice. Over one hundred spots were electroblotted for N-terminal sequencing. Among the newly sequenced proteins, 62 were from Arabidopsis and 51 from rice.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.1150170507
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  • 5
    Electronic Resource
    Electronic Resource
    Separation and characterization of rice proteins (1994)
    Weinheim : Wiley-Blackwell
    Electrophoresis 15 (1994), S. 708-720 
    Details
    ISSN: 0173-0835
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Rice proteins from nine tissues and one organelle (leaf, chloroplast, stem, root, germ, dark germinated seedling, seed, bran, chaff and callus) were isolated and then separated by two-dimensional gel electrophoresis (2-DE). The protein spots were characterized according to molecular weight, isoelectric point and partial amino-terminal sequence. Electrophoresis was carried out by isoelectric focusing (IEF), nonequilibrium pH gradient electrophoresis (NEPHGE) and immobilized pH gradient (IPG) in the first dimension, and by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) in the second dimension. With the aid of nine marker proteins, the patterns of IEF, NEPHGE and IPG 2-DE gels were graphically combined by computer into a single synthetic image for each tissue, respectively, and these images for the nine tissues and one organelle were again combined into a single 2-DE image for the integrated rice protein spots. The rice 2-DE gel image resolved 4892 proteins. About 3% of the spots are characterized by amino-terminal sequencing.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.1150150198
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