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  • complementation cloning  (2)
  • Kompensation unspezifischer Lichtverluste  (1)
  • inflammation  (1)
  • Springer  (4)
  • 1
    Electronic Resource
    Electronic Resource
    Nerve growth factor. A structural relationship between its proteolytic and leukocyte-chemotactic active sites (1985)
    Springer
    Molecular and cellular biochemistry 66 (1985), S. 65-69 
    Details
    ISSN: 1573-4919
    Keywords: inflammation ; wound healing ; serine proteases ; chemotaxis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Summary High molecular weight mouse nerve growth factor(H M W-NGF), in addition to its effects on certain neural elements, is also chemotactic for human polymorphonuclear leukocytes. One of the subunits of H M W-NGF is a protease of the serine family and its active site contains a serine residue and a closely-neighboring histidine residue that are both essential for proteolysis. Elimination of enzyme activity by irreversibly blocking the single serine has no effect on leukotaxis, but blocking the histidine abolishes leukotaxis. These results suggest the possibility that part of the proteolytic active site of this enzyme may have evolved to perform more than one, completely different, biologic function — proteolysis as well as nonproteolytically mediated chemotaxis.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00231825
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  • 2
    Electronic Resource
    Electronic Resource
    Identification of a cDNA that encodes a 1-acyl-sn-glycerol-3-phosphate acyltransferase from Limnanthes douglasii (1995)
    Springer
    Plant molecular biology 29 (1995), S. 267-278 
    Details
    ISSN: 1573-5028
    Keywords: 1-acyl-sn-glycerol-3-phosphate acyltransferase ; complementation cloning ; Limnanthes douglasii
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Two different techniques were used to isolate potential cDNAs for acyl-CoA: 1-acyl-sn-glycerol-3-phosphate acyltransferase (LPA-AT) enzymes from Limnanthes douglasii. Both heterologous screening with the maize pMAT1 clone and in vivo complementation of the Escherchia coli mutant JC201 which is deficient in LPA-AT activity, were carried out. Clones identified by these procedures were different. Homology searches demonstrated that the clone isolated by heterologous probing, pLAT1, encodes a protein which is most similar to the maize (open reading frame in pMAT1) and yeast SLC1 proteins, which are putative LPA-AT sequences. This L. douglasii sequence shows much lower homology to the E. coli LPA-AT protein PlsC, which is the only LPA-AT sequence confirmed by over-expression studies. The clone isolated by complementation, pLAT2, encodes a protein with homology to both SLC1 and PlsC. It was not possible to over-express the complementing protein encoded by pLAT2 but further experimentation on membranes from complemented JC201 demonstrated that they possess a substrate specificity distinctly different from PlsC and similar to Limnanthes sp. microsome specificity. This data strongly supports the contention that pLAT2 is an LPA-AT clone. Northern blot analysis revealed different expression patterns for the two genes in pLAT1 and pLAT2. Transcription of the gene encoding the insert of pLAT2 occurred almost exclusively in developing seed tissue, whilst the cDNA of pLAT1 hybridised to poly(A)+ mRNA from seed, stem and leaf, demonstrating more widespread expression throughout the plant. Southern blot analysis indicated that the cDNA of pLAT2 was transcribed from a single-copy gene while that for pLAT1 was a member of a small gene family.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00043651
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  • 3
    Electronic Resource
    Electronic Resource
    Isolation and characterisation of a maize cDNA that complements a 1-acyl sn-glycerol-3-phosphate acyltransferase mutant of Escherichia coli and encodes a protein which has similarities to other acyltransferases (1994)
    Springer
    Plant molecular biology 26 (1994), S. 211-223 
    Details
    ISSN: 1573-5028
    Keywords: maize ; 1-acyl-sn-glycerol-3-phosphate acyltransferase ; complementation cloning
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract We selected cDNA plasmid clones that corrected the temperature-sensitive phenotype of Escherichia coli strain JC201, which is deficient in 1-acyl-sn-glycerol-3-phosphate acyltransferase activity. A plasmid-based maize endosperm cDNA library was used for complementation and a plasmid that enabled the cells to grow at 44°C on ampicillin was isolated. Addition of this plasmid (pMAT1) to JC201 restored 1-acyl-sn-glycerol-3-phosphate acyltransferase activity to the cells. Total phospholipid labelling showed that the substrate for the enzyme, lysophosphatidic acid, accumulated in JC201 and was further metabolised to phosphatidylethanolamine in complemented cells. Membranes isolated from such cells were able to convert lysophosphatidic acid to phosphatidic acid in acyltransferase assays. The cDNA insert of pMAT1 contains one long open reading frame of 374 amino acids which encodes a protein of relative molecular weight 42 543. The sequence of this protein is most similar to SLC1, which is thought to be able to acylate glycerol at the sn-2 position during synthesis of inositol-containing lipids. Homologies between the SLC1 protein, the 1-acyl-sn-glycerol-3-phosphate acyltransferase of E. coli (PlsC) and the maize ORF were found with blocks of conserved amino acids, whose spacing was conserved between the three proteins, identifiable.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00039533
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  • 4
    Electronic Resource
    Electronic Resource
    Eine neuartige Methode der Kompensation unspezifischer Lichtverluste in der Atomabsorptions-Spektroskopie (1974)
    Springer
    Fresenius' Zeitschrift für analytische Chemie 272 (1974), S. 177-181 
    Details
    ISSN: 1618-2650
    Keywords: Best. von Blei in Milch, Blut ; Spektralphotometrie, Atomabsorption ; Kompensation unspezifischer Lichtverluste
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Description / Table of Contents: Zusammenfassung Es wird ein neuartiges System zur Kompensation unspezifischer Lichtverluste in der Atomabsorptions-Spektroskopie beschrieben. Dieses System hat folgende typische Eigenschaften: Es arbeitet im Zweistrahlbetrieb und gestattet die Ermittlung der unspezifischen und spezifischen Lichtverluste im gleichen Bereich der Atomzone. Sowohl sehr schnell veränderliche, als auch sehr hohe unspezifische Lichtverluste (bis zu mindestens 1,0 Extinktionseinheiten) können kompensiert werden. Als Anwendungsbeispiele werden die Bestimmung von Blei in Kondensmilch und in aufgeschlossenen Blutproben diskutiert.
    Notes: Abstract A new system is described with particular attention being given to the characteristic features: it works in the double beam mode and allows the determination of non-specific and specific losses of light in the same area of the atomic zone; a reliable compensation may be accomplished for quickly varying as well as for high non-specific losses of light (up to at least 1.0 absorbance units). The determinations of lead in condensed milk and in digested blood are discussed as typical examples for the application of the system.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00869174
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