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  • 1
    Electronic Resource
    Electronic Resource
    Pumpability of Residual Fuel Oils (1954)
    s.l. : American Chemical Society
    Industrial & engineering chemistry 46 (1954), S. 1264-1278 
    Details
    ISSN: 1520-5045
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology , Process Engineering, Biotechnology, Nutrition Technology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/ie50534a044
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Chemotaxis of lymphoblasts (1975)
    [s.l.] : Nature Publishing Group
    Nature 256 (1975), S. 646-648 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Locomotion and chemotaxis of blast-transformed lymphocytes were measured using the micropore filter technique as described previously8. For mouse lymphoblasts a filter of Sum pore size was used. Because the human blasts were larger, filters of 12 jam pore size (Sartorius, Gottingen, Germany) were ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/256646a0
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    Studies of chemotaxis of lymphocytes (1976)
    Springer
    Inflammation research 6 (1976), S. 243-247 
    Details
    ISSN: 1420-908X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Lymphoblasts migrate into filters towards chemoattractants in vitro. Human lymphoblasts maintained in continuous culture and mouse lymphoblasts from unsensitized lymph nodes show chemotactic responses and migrate towards the same chemotactic factors as neutrophils and macrophages, namely activated plasma, casein, denatured serum albumin, oxazolone. On the other hand, mouse lymphoblasts from oxazolone-sensitized lymph nodes show considerable randon migration and chemokinesis but not chemotaxis. The migration of lymphoblasts to these agents appears not to be antigen-specific. These migratory properties of lymphoblasts are probably relevant to their migration into inflammatory sites in vivo.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01972215
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  • 4
    Electronic Resource
    Electronic Resource
    Evolutionary genetics ofDrosophila esterases (1993)
    Springer
    Genetica 90 (1993), S. 239-268 
    Details
    ISSN: 1573-6857
    Keywords: Drosophila ; esterases ; multigene families ; structure function models
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Over 30 carboxylester hydrolases have been identified inD. melanogaster. Most are classified as acetyl, carboxyl or cholinesterases. Sequence similarities among most of the carboxyl and all the cholinesterases so far characterised fromD. melanogaster and other eukaryotes justify recognition of a carboxyl/cholinesterase multigene family. This family shows minimal sequence similarities with other esterases but crystallographic data for a few non-drosophilid enzymes show that the family shares a distinctive overall structure with some other carboxyl and aryl esterases, so they are all put in one superfamily of /β hydrolases. Fifteen esterase genes have been mapped inD. melanogaster and twelve are clustered at two chromosomal sites. The constitution of each cluster varies acrossDrosophila species but two carboxyl esterases in one cluster are sufficiently conserved that their homologues can be identified among enzymes conferring insecticide resistance in other Diptera. Sequence differences between two other esterases, the EST6 carboxyl esterase and acetylcholinesterase, have been interpreted against the consensus super-secondary structure for the carboxyl/cholinesterase multigene family; their sequence differences are widely dispersed across the structure and include substantial divergence in substrate binding sites and the active site gorge. This also applies when EST6 is compared across species where differences in its expression indicate a difference in function. However, comparisons within and among species where EST6 expression is conserved show that many aspects of the predicted super-secondary structure are tightly conserved. Two notable exceptions are a pair of polymorphisms in the substrate binding site of the enzyme inD. melanogaster. These polymorphisms are associated with differences in substrate interactionsvitro} and demographic data indicate that the alternative forms are not selectively equivalentin vivo.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01435043
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    Paper (German National Licenses)
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