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  • 1
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Fig. 1 Detection of the PUM polymorphism. The glycoproteins were separated by SDS 5-15% polyacrylamide gel electrophoresis (PAGE), transferred electrophoretically onto nitrocellulose, and detected using the monoclonal antibody Cal, as described pre-viously2. 0, Mendelian inheritance of the PUM ...
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  • 2
    Electronic Resource
    Electronic Resource
    [s.l.] : Nature Publishing Group
    Nature 269 (1977), S. 261-262 
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Treatment of extracts of various human tissues with the enzvme neuraminidase (sialidase) seems to result in the conversion of the most anodal tissue ADA isozymes (CL h and c) into a zone of activity (d2) which is slightly less anodal than the major Jisozymc (now referred toas/,). The effects of ...
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  • 3
    ISSN: 1573-4927
    Keywords: nucleoside monophosphate kinases ; enzyme decay ; red cell aging ; allelic variation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract The nucleoside monophosphate kinases, adenylate kinase (AK), guanylate kinase (GUK), and uridine monophosphate kinase (UMPK), were studied electrophoretically and quantitatively in density gradient fractions of human red cells from normal adults which contain red cells of differing mean age. The enzymes were found to differ both in their rates and patterns of decay and in secondary isozyme formation during the life of the red cell in the circulation. AK showed no appreciable enzyme decay and slight generation of secondary isozymes; UMPK showed a rapid monophasic decline and no secondary isozyme formation; GUK showed intermediate overall loss of activity with a biphasic pattern of decay and marked secondary isozyme formation. A comparative study of the two common phenotypes of UMPK (UMPK 1 and UMPK 2-1) and of AK (AK 1 and AK 2-1) was made. The UMPK 2 isozyme showed a more rapid decay than the UMPK 1 isozyme, whereas no difference was observed between the AK 1 and AK 2 isozymes.
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  • 4
    ISSN: 1573-4927
    Keywords: human lactase ; purification ; monoclonal antibody ; polyclonal antibodies ; immunology of lactase persistence
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract Human lactase purified from detergent extracts of the total membrane fraction of postmortem jejunum by means of monoclonal immunoadsorbent chromatography appears to be a dimer of subunits identical in Mr (160K). Trypsin or papain removes a small hydrophobic anchoring peptide from each subunit to give a hydrophilic enzyme which no longer interacts with detergent micelles. Lactase hydrolyzes, besides lactose, cellobiose and the synthetic substrates, 4-methylumbelliferyl-β-galactoside and β-glucoside, as well as phlorizin; but it does not hydrolyze glucocerebroside. Phlorizin hydrolase is associated with lactase under all conditions investigated; coincident staining on immunodiffusion and immunoelectrophoresis, coincident elution on immunoadsorbent chromatography and on gel filtration in a dissociating buffer, and correlated reduction in activity in lactase-nonpersistent individuals. Adult and infant lactases are indistinguishable by titration or immunodiffusion against polyclonal rabbit antibodies. Adult individuals low in lactase activity also show a corresponding reduction in cross-reacting material. These observations suggest that lactase persistence is due to the continued synthesis of the infant enzyme.
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  • 5
    ISSN: 1573-6865
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Purified lactate dehydrogenase (LDH) isoenzyme 1 (H or B subunits) and isoenzyme 5 (M or A subunits) were used to prepare monoclonal antibodies (MAb) suitable for immunohistochemical detection on formalin fixed paraffin-embedded tissue sections. In the initial fusions, screening of the antibodies was based on enzyme linked immunosorbent assay (ELISA) against the immunogens. None of the antibodies obtained was satisfactory. There were various problems related to specificity, crossreactivity, affinity and also the properties of the monoclonal antibody itself. Using a combined system involving more than one method for screening, two suitable monoclonal antibodies, MAb65 (to H-type LDH) and MAb25 (to M-type LDH) were selected. Both antibodies reacted specifically with corresponding LDH isoenzymes as shown in a series of tests. Their reactivity in sections of formalin fixed paraffin-embedded tissue indicated that both antibodies are suitable reagents for immunohistochemical studies.
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  • 6
    ISSN: 1572-9931
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract A panel of microcell hybrids containing fragments of chromosome 2 was analyzed for the presence of humanDPP4, the gene that codes for dipeptidyl peptidase IV (or CD26), by specific PCR amplification of a fragment of the 3′ untranslated region of the gene. This analysis placedDPP4 betweenLCT andGAD in bands q21 to q31. The localization was confirmed by in situ hybridization using two genomic probes that each revealed a hybridization signal in band q24. We also use the recent identification of the ADA binding protein as DPPIV to propose that the geneADCP2 should be renamedDPP4.
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  • 7
    Electronic Resource
    Electronic Resource
    Springer
    Glycoconjugate journal 1 (1984), S. 183-190 
    ISSN: 1573-4986
    Keywords: Tamm-Horsfall glycoprotein ; Sd a antigen ; 125 I lectins ; soy-bean agglutinin ; SDS-gel electrophoresis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract Preparations of Tamm-Horsfall glycoprotein were examined by SDS-polyacrylamide gel electrophoresis and detection using various125I-lectins as well as Coomassie Brilliant Blue. Considerable heterogeneity of electrophoretic pattern was seen. This was not due to a genetic polymorphism. Variation in binding by Soy-bean agglutinin was also seen. This was correlated with the Sda phenotype of the individual.
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