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  • 1
    Electronic Resource
    Electronic Resource
    Restriction polymorphisms of the ceruloplasmin gene on chromosome 3 (1995)
    Springer
    Human genetics 〈Berlin〉 96 (1995), S. 239-240 
    Details
    ISSN: 1432-1203
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract Using a probe isolated from a human liver cDNA library, polymorphisms were observed in the human ceruloplasmin gene with the enzymes PstI and MspI. The PstI polymorphism was frequent (allele frequencies, 0.46 and 0.54) whereas the polymorphisms found with MspI were rare.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00207390
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  • 2
    Electronic Resource
    Electronic Resource
    A transcriptional analysis of the S1Bn (Brassica napus) family of SINE retroposons (1996)
    Springer
    Plant molecular biology 32 (1996), S. 869-878 
    Details
    ISSN: 1573-5028
    Keywords: repetitive sequence ; reverse transcriptase ; Alu element ; transposable element ; retroelement
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract S1Bn is a plant short interspersed element (SINE) whose amplification probably involves the reverse transcription of an RNA intermediate. In this report, we identified and characterized S1Bn transcripts from different Brassica napus tissues. Despite the presence of a consensus internal POL III promoter in a large number of genomic S1Bn elements, we observed that S1Bn transcripts are rare in B. napus cells. The use of two very sensitive methods (RT-PCR and RACE PCR) allowed the characterization of 102 independent S1Bn cDNA clones from three different tissues (shoot, root and callus). From this analysis, we conclude that the majority of S1Bn transcripts probably result from a small number of cotranscriptional events where an S1Bn element is transcribed due to its presence in a POL II transcriptional unit. Specific POL III RNA transcripts, initiating at the first 5′ nucleotide of the DNA element, are also present in the tested tissues and possibly result from the transcriptional activity of as few as three genomic elements. Two of these transcripts could represent master transcripts responsible for the amplification of S1Bn subfamilies. We also observed that the population of specific POL III transcripts varies among the three tested tissues and that some transcripts appear completely tissue-specific.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00020484
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  • 3
    Electronic Resource
    Electronic Resource
    S1 SINE retroposons are methylated at symmetrical and non- symmetrical positions in Brassica napus: identification of a preferred target site for asymmetrical methylation (1999)
    Springer
    Plant molecular biology 39 (1999), S. 243-255 
    Details
    ISSN: 1573-5028
    Keywords: Alu ; methylation ; CpG ; retroposon ; Cruciferae
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract DNA methylation has been often proposed to operate as a genome defence system against parasitic mobile elements. To test this possibility, the methylation status of a class of plant mobile elements, the S1Bn SINEs, was analysed in detail using the bisulfite modification method. We observed that S1Bn SINE retroposons are methylated at symmetrical and asymmetrical positions. Methylated cytosines are not limited to transcriptionally important regions but are well distributed along the sequence. S1Bn SINE retroposons are two-fold more methylated than the average methylation level of the Brassica napus nuclear DNA. By in situ hybridization, we showed that this high level of methylation does not result from the association of S1Bn elements to genomic regions known to be highly methylated suggesting that S1Bn elements were specifically methylated. A detailed analysis of the methylation context showed that S1Bn cytosines in symmetrical CpG and CpNpG sites are methylated at a level of 87% and 44% respectively. We observed that 5.3% of S1Bn cytosines in non- symmetrical positions were also methylated. Of this asymmetrical methylation, 57% occurred at a precise motif (Cp(A/T)pA) that only represented 12% of the asymmetrical sites in S1Bn sequences suggesting that it represents a preferred asymmetrical methylation site. This motif is methylated in S1Bnelements at only half the level observed for the Cp(A/T)pG sites. We show that non-S1Bn CpTpA sites can also be methylated in DNA from B. napus and from other plant species.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1006108325504
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  • 4
    Electronic Resource
    Electronic Resource
    Rapid purification of native SecA fromEscherichia coli: Development of a new affinity chromatography procedure (1994)
    Springer
    Current microbiology 29 (1994), S. 323-329 
    Details
    ISSN: 1432-0991
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract The SecA protein occupies a pivotal position in the public protein export pathway inEscherichia coli. The multifunctional SecA protein recognizes cytoplasmic factors associated with export including the presecretory protein and targets the complex to the inner membrane, where it acts in the early stages of protein translocation. The ability of SecA to bind ATP was the basis for the development of a novel, rapid purification scheme involving a single chromatographic step. Affinity chromatography was carried out on Red Sepharose CL-6B. The SecA present in crude extracts ofE. coli binds strongly to this dye-ligand matrix, and active protein was purified to greater than 90% homogeneity. The protein isolated by this procedure retained the previously described ATPase and RNA-binding activities of SecA. This approach should permit the rapid purification of SecA homologs from a variety microorganisms.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01570224
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  • 5
    Electronic Resource
    Electronic Resource
    Silver stain after isoelectric focusing of unconcentrated cerebrospinal fluid: Visualization of total protein and direct immunofixation of immunoglobulin G (1982)
    Weinheim : Wiley-Blackwell
    Electrophoresis 3 (1982), S. 206-209 
    Details
    ISSN: 0173-0835
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: A silver stain technique has been developed to study proteins in unconcentrated cerebrospinal fluid (CSF) after isoelectric focusing. This method is highly sensitive, and bands containing 25 to 50 ng protein can be clearly distinguished, so that small volumes (40 μl maximum) of native CSF can be used. Individual proteins (e. g., immunoglobulin G) can be detected easily by specific immunofixation. It is also possible to perform direct precipitation and direct specific immunofixation on a single gel in order to compare side by side the patterns of the whole and of specific proteins from different samples of CSF. The technique is simple and highly reproducible, and results are obtained 6 h after sample deposition (if immunofixation is used, a further 24 h washing is necessary). The sensitivity and versatility of this technique (immunofixation can be applied to the detection of any antigen) should permit its extension to other biological fluids with a low protein content.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.1150030405
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  • 6
    Electronic Resource
    Electronic Resource
    Electrophoretic demonstration of interactions between group specific component (vitamin D binding protein), actin, and 25-hydroxycholecalciferol (1984)
    Weinheim : Wiley-Blackwell
    Electrophoresis 5 (1984), S. 22-26 
    Details
    ISSN: 0173-0835
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Group specific component (Gc) is known to interact with both vitamin D3 metabolites and actin. The present study was undertaken to determine if analytical isoelectric focusing could form the basis of a simple and reliable method for discriminating native Gc and complexes with 25-hydroxycholecalciferol (25(OH)D3) from those formed with actin and with both ligands. Increasing amounts of G-actin and/or 25(OH)D3 were added to purified Gc of both Gc1 and Gc2 phenotypes. Actin and 25(OH)D3 interacted independently and simultaneously with native Gc, giving rise to three different complexes of increasing acidity: Gc-25(OH)D3, Gc-actin, and actin-Gc-25(OH)D3, which were clearly resolved from the native Gc protein and from each other. In addition, the inherent differences in microheterogeneity and polymorphism between the two major phenotypes examined (Gc1 and Gc2) were also retained in their respective complexes. Similar results were obtained upon addition of 25(OH)D3 or actin to whole human serum, the bands corresponding to native or complexed Gc being recognized in this case by print immunofixation. These results indicate that complexes formed between Gc protein and both 25(OH)D3 and actin can be clearly detected and resolved by electrophoretic procedures.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.1150050104
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  • 7
    Electronic Resource
    Electronic Resource
    Horizontal two-dimensional (iso-dalt) electrophoresis: Use of agarose isoelectric focusing and SDS gel electrophoresis in an exponential gradient for characterization of plasma proteins (1980)
    Weinheim : Wiley-Blackwell
    Electrophoresis 1 (1980), S. 159-163 
    Details
    ISSN: 0173-0835
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: The two-dimensional (iso-dalt) electrophoresis system for protein separation has been modified to include the use of flat-bed agarose isoelectric focusing in the first dimension, horizontal SDS-electrophoresis in an exponential acrylamide gradient in the second dimension, molecular weight standards run side by side with the sample in the SDS-polyacrylamide gel, and radiolabeled proteins as internal standards. Direct determination of the pH gradient after the first dimension and of molecular weights after the second dimension permits more accurate measurement of the protein spots in both the x and y axes, thus improving the confidence limits of the technique. The reproducibility of molecular weight determinations was calculated for eight different proteins in six different gels, with an overall standard deviation of 3.02%. Incorporation of internal standards is useful in identifying and confirming protein patterns. Examples of the application of this technique to the separation of specific plasma proteins are described.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.1150010307
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  • 8
    Electronic Resource
    Electronic Resource
    Isolectric patterns of human alpha1- antichymotrypsin (A1AChy) and A1AChy-protease complexes (1981)
    Weinheim : Wiley-Blackwell
    Electrophoresis 2 (1981), S. 247-250 
    Details
    ISSN: 0173-0835
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: When studied by thin-layer polyacrylamide gel isoelectric focusing, alpha1-an-tichymotrypsin (A1AChy) in human plasma presents a microheterogeneous pattern, consisting of seven bands with isoelectric points (pI) between 4.1 and 4.45. After removal of sialic acids by neuraminidase treatment, four bands are seen with a more alkaline pI (about 1.0 pH unit). Thus, the microheterogeneity of human A1AChy is due only in part to differential sialylation of the isoproteins. Incubation of A1AChy (in excess) with alpha-chymotrypsin results in the formation of a primary complex. In the presence of excess protease, incubation results in a secondary complex with a lower pI. Upon incubation of A1AChy with trypsin, no protease-inhibitor complexes are observed, although there is evidence for partial degradation of the A1AChy molecule.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.1150020409
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  • 9
    Electronic Resource
    Electronic Resource
    Pseudo-ligand affinity chromatography and high-voltage isoelectric focusing as a multiparameter method for separation and identification of plasma proteins (1983)
    Weinheim : Wiley-Blackwell
    Electrophoresis 4 (1983), S. 205-211 
    Details
    ISSN: 0173-0835
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: A system is described that utilizes physical-chemical characteristics of macromolecules, not restricted to charge-size variations, for the separation of the plasma proteins. The first step, using pseudo-ligand affinity chromatography, separates the plasma proteins into fractions which were characterized by fused rocket immuno-electrophoresis. Then electrophoresis in the form of high voltage gradient isoelectric focusing on ultrathin-layer polyacrylamide gels is employed to further separate each of the fractions by charge differences. The advantages of this technique are that the proteins are maintained without noticeable denaturation, allowing a variety of direct functional tests. One is not restricted to only charge-size variations for separation and the technique is a preparative-to-analytical procedure. Furthermore, the higher voltage gradients employed increase resolution of proteins significantly and require separation times of only 30-35 min. The limit of detectability is 50 μg/dl of protein, using silver diamine staining. The feasibility of this and related techniques as applied to the study of genetic polymorphisms and as an aid in the correlation and identification of spots obtained in dissociating-denaturing two-dimensional electrophoresis methods is emphasized.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.1150040304
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  • 10
    Electronic Resource
    Electronic Resource
    Electrophoretic and isoelectric focusing analysis of human recombinant alpha2-HS glycoprotein produced in insect cells: Analysis of the post-translational events (1996)
    Weinheim : Wiley-Blackwell
    Electrophoresis 17 (1996), S. 529-532 
    Details
    ISSN: 0173-0835
    Keywords: Isoelectric focusing ; Alpha2-HS glycoprotein ; Baculovirus expression system ; Posttranslational modifications ; Insulin receptor tyrosine kinase ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Alpha2-HS glycoprotein (AHSG) is a human serum glycoprotein synthesized by liver cells. It is a natural inhibitor of the insulin receptor tyrosine kinase activity. We produced this protein in insect cells by using a recombinant baculovirus expressing the whole coding sequence of the protein. By analyzing AHSG on isoelectric focusing and on sodium dodecyl sulfate (SDS) gels, followed by immunoblot, AHSG produced in insect cells was found to be phosphorylated and to possess the connecting peptide between the A and the B chains. The same features were found in the protein produced by Hep3B, a human liver cell line that synthesizes AHSG. By contrast, no phosphorylation could be detected in AHSG present in normal human plasma, and the connecting peptide was clipped. As the protein produced in insect cells is active on insulin receptors, in contrast to the plasma protein, our results suggest that the biological activity of the protein may be associated with its single chain form together with its phosphorylation.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.1150170320
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