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  • 1
    Electronic Resource
    Electronic Resource
    Radioimmunologische Bestimmung von 25-Hydroxycholecalciferol (1976)
    Springer
    Microchimica acta 66 (1976), S. 161-173 
    Details
    ISSN: 1436-5073
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Description / Table of Contents: Summary The antibody to vitamin D3 as hapten proved useful in determination of 25-hydroxycalciferol (25-OH-CC). The attempt also to determine vitamin D3 directly with the aid of this radioimmunological procedure failed because of the poor solubility of the vitamin in aqueous systems. Because of the linkage to the C3 the D-ring and C17 side chain would be expected to be the immunodeterminant sites. Although the antibody can be used to determine 25-OH-CC, there is no cross-reaction with cholesterol. This indicates the importance of the open B-ring of this vitamin. Scrutiny of the method showed good reproducibility and accuracy. The most favorable evaluation region is 0.1–2 ng/250μl sample. The procedure described enables 25hydroxy vitamin D3 to be determined without previous purification of the sample extract.
    Notes: Zusammenfassung Der gegen Vitamin D3 als Hapten gerichtete Antikörper bewährte sich bei der Bestimmung von 25-OH-Cholecalciferol (25-OH-CC). Der Versuch, auch Vitamin D3 mit Hilfe dieses radioimmunologischen Verfahrens direkt zu bestimmen, scheiterte an der schlechten Löslichkeit des Vitamins in wäßrigen Systemen. Auf Grund der Kopplung an das C-Atom-3 wären der D-Ring und die C-17-Seitenkette als immundeterminante Stellen zu erwarten. Die Tatsache, daß der Antikörper zur Bestimmung des 25-OH-CC herangezogen werden kann, gleichzeitig aber keine Kreuzreaktion mit Cholesterin ergibt, weist auf die Bedeutung des offenen B-Ringes dieser Vitamine hin. Die Überprüfung der Methode ergab gute Reproduzierbarkeit und Genauigkeit. Der günstigste Auswertebereich liegt bei 0,1–2 ng/250μl Ansatz. Das beschriebene Verfahren ermöglicht die Bestimmung von 25-Hydroxy-Vitamin-D3 ohne vorherige Reinigung des Probenextraktes.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01257106
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  • 2
    Electronic Resource
    Electronic Resource
    Zur Synthese von Human-Big-Gastrin I und seinem 32-Leucin-Analogon (1980)
    Springer
    Monatshefte für Chemie 111 (1980), S. 125-141 
    Details
    ISSN: 1434-4475
    Keywords: Human big gastrin I ; Leu32-human big gastrin I ; Synthetic peptide hormones
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract The preparation of the pure tetratriacontapeptide amide 〈Glu-Leu-Gly-Pro-Gln-Gly-His-Pro-Ser-Leu-Val-Ala-Asp-Pro-Ser-Lys-Lys-Gln-Gly-Pro-Trp-Leu-Glu-Glu-Glu-Glu-Glu-Ala-Tyr-Gly-Trp-Met-Asp-Phe-NH2 (human big gastrin I) and the analogue Leu32-human big gastrin I from the crude synthetic materials obtained after deblocking of the overall protected tetratriacontapeptide amide derivatives by means of trifluoroacetic acid is described. The criteria for homogeneity obtained by chromatographic, electrophoretic, enzymatic and spectroscopic methods are reported.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00938723
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  • 3
    Electronic Resource
    Electronic Resource
    Two-dimensional electrophoresis in small gels for applications in veterinary medicine (1991)
    Weinheim : Wiley-Blackwell
    Electrophoresis 12 (1991), S. 303-306 
    Details
    ISSN: 0173-0835
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: A versatile method for two-dimensional electrophoresis that can be performed easily, even in small routine laboratories, is described. The procedure combines a first-dimensional isoelectric focusing run in a PhastSystem with denaturing electrophoresis in a small vertical electrophoresis chamber. The described arrangement of two first-dimensional gel strips in the second dimension allows direct comparison of two related samples, eliminating most of the artifacts that usually lead to misinterpretations. The presented procedure can be conveniently adapted to the needs of each laboratory; at present, it is being extensively used to establish proteir patterns of healthy individuals of different species, a prerequisite with regard to help and support diagnosis.
    Additional Material: 1 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.1150120413
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  • 4
    Electronic Resource
    Electronic Resource
    Proteins of rat serum: II. Influence of some biological parameters of the two-dimensional electrophoresis patternProtein identifications in rat serum 2-DE map (according to Fig. 2A and Table 1) and linkages to OWL data base [1] can be reached through the Aebersold lab web site at: http://weber.u.washington.edu/∼ruedilab/aebersold.html. (1998)
    Weinheim : Wiley-Blackwell
    Electrophoresis 19 (1998), S. 1493-1500 
    Details
    ISSN: 0173-0835
    Keywords: Rat serum ; Two-dimensional polyacrylamide gel electrophoresis ; Inflammation ; Thyroid ; Affinity chromatography ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: This report complements the database already detailed for serum proteins of healthy adult male rats (P. Haynes et al., Electrophoresis 1998, 19, 1484-1492). The influence on the two-dimensional electrophoresis (2-DE) pattern of certain physiological conditions (sex, age) was studied as well as of changes in thyroid metabolism. We have extended the information about the major components of rat serum by identifying the proteins typical for the response to acute inflammation. Analyzing 27 spots, six proteins not found in control sera could be recognized; migration at overlapping or close positions with five already characterized proteins was observed for some. A compilation of all our rat data can be accessed through: ////http://weber.u.washington.edu/∼ruedilab/aebersold.html.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.1150190846
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  • 5
    Electronic Resource
    Electronic Resource
    Ultrathin-layer isoelectric focusing of enzymes in liver samples of wagtails (Motacilla flava, ssp.) (1982)
    Weinheim : Wiley-Blackwell
    Electrophoresis 3 (1982), S. 146-151 
    Details
    ISSN: 0173-0835
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Wagtail samples (Motacilla flava, ssp; song bird) have been collected in different regios of central and southern Europe. Due to sampling extending over long periods of time it was necessary to investigate the effect of storing conditions (liquid nitrogen or -36 °C). Isozyme separation was done by polyacrylamide ultrathinlayer isoelectric focusing (100 μm). Liver homogenates were diluted in appropriate manner and 5 μl aliquots were used for separations. Gels for isoelectric focusing (T = 5.4, C = 2.8) containing different kinds of carrier ampholytec (Servalyt, Pharmalyte and Ampholines were cast on 12.5 × 20 cm pretreated glass plates according to the procedure of Radola [9]. Enzyme staining was performed in solution (ACP and esterases) or with an agarose overlay technique (LDH, ADH, MDH, PGM and GPI). Wagtail liver samples were chosen to optimize the electrophoretic conditions and to test the usefulness of different staining methods. This  -  and investigations presently under way on samples of pectoral muscle, heart, brain and blood  -  should allow us to elucidate genetic differences at the molecular level of the various subspecies of wagtails. The smaller total amount of protein available in some of these samples stresses the necessity of choosing a reproducible and sensitive, as well as rapid, electrophoretic technique.
    Additional Material: 8 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.1150030306
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  • 6
    Electronic Resource
    Electronic Resource
    Peculiarities in electrophoretic behavior of different serum albumins (1993)
    Weinheim : Wiley-Blackwell
    Electrophoresis 14 (1993), S. 1312-1317 
    Details
    ISSN: 0173-0835
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Behavior of serum albumins of different species was compared with regard to electrophoretic mobility under native conditions, molecular mass and isoelectric point in presence or absence of denaturing agents. In addition to serum samples from human, horse, cow, pig, cat, dog, sheep, goat, chicken, rabbit, mouse, and rat, commercially available standards or albumin preparations obtained by chromatographic procedures were analyzed. Feline and canine albumins showed marked differences in all investigated methods. Our experiments also revealed several factors influencing albumin patterns, especially during isoelectric focusing in immobilized pH gradients or in the presence of carrier ampholytes.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.11501401201
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  • 7
    Electronic Resource
    Electronic Resource
    An electrophoretic study on interactions of albumins of different species with immobilized Cibacron Blue F3G A (1998)
    Weinheim : Wiley-Blackwell
    Electrophoresis 19 (1998), S. 2506-2514 
    Details
    ISSN: 0173-0835
    Keywords: Affinity electrophoresis ; Titration curves ; Albumin ; Animal species ; Cibacron Blue ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Albumins of different species, varying in electrophoretic mobility, were compared in their interaction with the dye Cibacron Blue F3G A. Immobilized by coupling to a high molecular weight dextran (“blue dextran”), the dye was used as a ligand in affinity electrophoresis in different setups. One-dimensional electrophoresis with blue dextran entrapped in an intermediate gel and two-dimensional applications with transverse gradients (affinity titration curves, zonal electrophoresis in linear ligand gradients) were performed. Compared to the human homologue, animal albumins display more complex patterns and interaction profiles, depending on pH and ionic strength of the buffers. Results may differ considerably from those obtained by affinity chromatography, illustrating the additional screening potential of the electrophoretic methods. Comparison of different samples under the influence of ligand competition, reducing conditions, or denaturing agents gives supplementary information on conformational behavior of the proteins.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.1150191425
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  • 8
    Electronic Resource
    Electronic Resource
    Proteins of rat serum: I. Establishing a reference two-dimensional electrophoresis map by immunodetection and microbore high performance liquid chromatography-electrospray mass spectrometryProtein identifications in rat serum 2-DE map (according to Fig. 2A and Table 1) and linkages to OWL database [1] can be reached through the Aebersold lab web site at: http://weber.u.washington.edu/∼ruedilab/aebersold.html. (1998)
    Weinheim : Wiley-Blackwell
    Electrophoresis 19 (1998), S. 1484-1492 
    Details
    ISSN: 0173-0835
    Keywords: Rat serum ; Two-dimensional polyacrylamide gel electrophoresis ; Electrospray mass spectrometry ; Microbore liquid chromatography ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: In the present investigation, we have identified 56 major spots, or spot rows, corresponding to 22 proteins, in the 2-DE pattern of adult male rats. This was done mainly by applying two complementary techniques, namely immunoblotting and high performance liquid chromatography-mass spectrometry (HPLC-MS) peptide mapping. Glycoproteins were characterized by affinity blotting with six lectins. We have also detailed how rat serum differs from human serum in two main respects: (i) relative abundance of individual proteins, which amounts in some cases to a complete absence in either sample, and (ii) varying molecular parameters for homologous proteins. It was thus possible to establish a first-generation reference map of rat serum proteins, which can be accessed through http://weber.u.washington.edu/∼ruedilab/aebersold.html. We hope the present database will be a useful reference for the evaluation of changes in serum protein distribution in the course of pharmacological and toxicological studies. The recognition of species-specific proteins appears of special relevance in this respect.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.1150190845
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  • 9
    Electronic Resource
    Electronic Resource
    Forensics on wild animals: Differentiation between otter and pheasant blood using electrophoretic methods (1995)
    Weinheim : Wiley-Blackwell
    Electrophoresis 16 (1995), S. 865-868 
    Details
    ISSN: 0173-0835
    Keywords: Species identification ; Pheasant ; Otter ; Forensic sciences ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Electrophoretic techniques were used to prove illegal hunting of a protected species as small amounts of dried blood stains could be clearly identified as of otter origin. Species differentiation between the otter (Lutra lutra) and pheasant (Phasianus colchicus) was based mainly on small differences in electrophoretic mobilities of the respective albumins and hemoglobins in one-dimensional separations. Additional differences in minor proteins of the two species were revealed by two-dimensional electrophoresis. Electrophoresis thus also proved to be a valuable tool for forensic purposes.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.11501601143
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  • 10
    Electronic Resource
    Electronic Resource
    Two-dimensional electrophoresis of cat sera: Protein identification by cross reacting antibodies against human serum proteins (1992)
    Weinheim : Wiley-Blackwell
    Electrophoresis 13 (1992), S. 450-453 
    Details
    ISSN: 0173-0835
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: After two-dimensional electrophoresis of cat serum, individual proteins were identified by means of cross reacting antibodies against the human protein homologues. Testing by cross reactivities seemed the method of choice because immunoreagents for cat proteins are not easily available.
    Additional Material: 1 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.1150130193
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