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  • 1
    Electronic Resource
    Electronic Resource
    Origin of the Isoelectric Heterogeneity of Monoclonal Immunoglobulin h1B4 (1993)
    Springer
    Pharmaceutical research 10 (1993), S. 1580-1586 
    Details
    ISSN: 1573-904X
    Keywords: microheterogeneity ; monoclonal antibody ; deamidation ; isoelectric focusing
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract The origin of the microheterogeneity of a highly purified antiinflammatory humanized monoclonal antibody prepared in mammalian cell culture has been investigated. This antibody is an IgG directed toward human CD 18 (a subunit of leukocyte integrins). When the IgG preparation is subjected to isoelectric focusing, it is found to contain four major species with pI values ranging from 6 to 7. Although the relative amounts of each form differ and some species are present only in small quantities, each has been isolated by a combination of high-resolution anion-exchange chromatography and isoelectric focusing. Comparative studies reveal no detectable differences in overall secondary (far UV circular dichroism) or tertiary (intrinsic fluorescence) structure, molecular weight (laser-desorption mass spectroscopy), or antigen binding activity. When each of the isolated species is incubated under conditions which favor deamidation, it is converted to forms of lower pI which appear to correspond to naturally observed species. While the isolated light chain is relatively homogeneous, the heavy chain exhibits a pattern of isoelectric focusing bands similar to that of the intact immunoglobulin. These results suggest that in this case, charge microheterogeneity is due to the sequential deamidation of the immunoglobulin heavy chain.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1018912417607
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Formulation Design of Acidic Fibroblast Growth Factor (1993)
    Springer
    Pharmaceutical research 10 (1993), S. 649-659 
    Details
    ISSN: 1573-904X
    Keywords: acidic flbroblast growth factor ; protein stability ; polyanions ; protein formulation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract The design of an aqueous formulation for acidic fibroblast growth factor (aFGF) requires an understanding of the type of compounds that can either directly or indirectly stabilize the protein. To this end, spectrophotometric turbidity measurements were initially employed to screen the ability of polyanionic ligands, less specific compounds, and variations in solution conditions (temperature and pH) to stabilize aFGF against heat-induced aggregation. It was found that in addition to the well-known protection of aFGF by heparin, a surprisingly wide variety of polyanions (including small sulfated and phosphorylated compounds) also stabilizes aFGF. These polyanionic ligands are capable of raising the temperature at which the protein unfolds by 15–30°C. Many commonly used excipients were also observed to stabilize aFGF in both the presence and the absence of heparin. High concentrations of some of these less specific agents are also able to increase the temperature of aFGF thermal unfolding by as much as 6–12°C as shown by circular dichroism and differential scanning calorimetry. Other compounds were found which protect the chemically labile cysteine residues of aFGF from oxidation. Aqueous formulations of aFGF were thus designed to contain both a polyanionic ligand that enhances structural integrity by binding to the protein and chelating agents (e.g., EDTA) to prevent metal ion-catalyzed oxidation of cysteine residues. While room-temperature storage (30°C) leads to rapid inactivation of aFGF in physiological buffer alone, several of these aFGF formulations are stable in vitro for at least 3 months at 30°C. Three aFGF topical formulations were examined in an impaired diabetic mouse model and were found to be equally capable of accelerating wound healing.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1018939228201
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  • 3
    Electronic Resource
    Electronic Resource
    Chemical crosslinking of cell membranes (1983)
    Springer
    Molecular and cellular biochemistry 50 (1983), S. 115-141 
    Details
    ISSN: 1573-4919
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Summary The complexity of cell membranes makes the resolution of their macromolecular topology one of the more challenging problems in modern molecular and cellular biochemistry. Despite the difficulties inherent in any such analysis, a surprisingly simple yet powerful approach exists that has consistently yielded valuable results. This method is chemical crosslinking, in which cell membranes are treated with crosslinking reagents (usually bifunctional) which produce covalent linkages between membrane components. The resultant complexes are usually then separated and identified by electrophoresis. This review is intended to provide a guide to the i.nvestigator who is unfamiliar with this approach. The overall strategy of crosslinking is discussed including selection of reagents, conditions to optimize crosslinking and the cleavage of crosslinked complexes to regenerate the original target for identification purposes. The crosslinking of biological membranes is then reviewed with special emphasis on recent advances including macromolecular photoaffinity labeling, kinetic analysis to probe symmetry properties and potential artifacts that may complicate interpretation of results. Examples of specific applications of crosslinking to membranes are presented in tabular form. The final portion of the review discusses the synthesis and properties of the most widely employed crosslinking reagents. Available reagents are summarized in a series of comprehensive tables. It is hoped that our discussion will provide the uninitiated investigator with sufficient information to ascertain the applicability of chemical crosslinking to particular areas of interest.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00285638
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  • 4
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    High-Throughput Biophysical Analysis of Protein Therapeutics to Examine Interrelationships Between Aggregate Formation and Conformational Stability (2013)
    Springer
    Details
    Publication Date: 2013-10-31
    Print ISSN: 1522-1059
    Electronic ISSN: 1550-7416
    Topics: Chemistry and Pharmacology
    Published by Springer
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