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  • Cholecystokinin-like peptide  (2)
  • Saccharomyces cerevisiae  (2)
  • 46L55  (1)
  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Letters in mathematical physics 35 (1995), S. 375-383 
    ISSN: 1573-0530
    Keywords: 46L55 ; 28D20 ; 82B10
    Source: Springer Online Journal Archives 1860-2000
    Topics: Mathematics , Physics
    Notes: Abstract We present a rigorous computation of the dynamical entropyh of the quantum Arnold cat map. This map, which describes a flow on the noncommutative two-dimensional torus, is a simple example of a quantum dynamical system with optimal mixing properties, characterized by Lyapunov exponents ± 1n λ+, λ+ 〉 1. We show that, for all values of the quantum deformation parameter,h coincides with the positive Lyapunov exponent of the dynamics.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1432-0983
    Keywords: α-Amylase ; Lipomyces kononenkoae ; LKA1 ; Saccharomyces cerevisiae
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract A highly active α-amylase (76 250 Da) secreted by the raw starch-degrading yeast Lipomyces kononenkoae strain IGC4052B was purified and characterized. Using high performance liquid chromatography (HPLC), end-product analysis indicated that the L. kononenkoae α-amylase acted by endo-hydrolysis on glucose polymers containing α-1,4 and α-1,6 bonds, producing mainly maltose, maltotriose and maltotetraose. The following NH2-terminal amino acids were determined for the purified enzyme: Asp-Cys-Thr-Thr-Val-Thr-Val-Leu-Ser-Ser-Pro-Glu-Ser-Val-Thr-Gly. The L. kononenkoae α-amylase-encoding gene (LKA1), previously cloned as a cDNA fragment, was expressed in Saccharomyces cerevisiae under the control of the PGK1 promoter. The native signal sequence efficiently directed the secretion of the glycosylated protein in S. cerevisiae. De-glycosylation of the enzyme indicated that post-translational glycosylation is different in S. cerevisiae from that in L. kononenkoae. Zymogram analysis indicated that glycosylation of the protein in S. cerevisiae had a negative effect on enzyme activity. Southern-blot analysis revealed that there is only a single LKA1 gene present in the genome of L. kononenkoae.
    Type of Medium: Electronic Resource
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  • 3
    ISSN: 1432-0878
    Keywords: Insect nervous system ; Cholecystokinin-like peptide ; Immunohistochemistry ; Radioimmunoassay ; Aeschna cyanea (Insecta)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Gastrin/cholecystokinin (gastrin/CCK)-like immunoreactivity has been detected in the brain, suboesophageal ganglion and corpora cardiaca of the larva of Aeschna cyanea by radioimmunoassay and immunohistochemistry, by use of two antisera raised against the sulfated (CCK-8S) and the unsulfated form (CCK-8NS) of the carboxyl terminal octapeptide. Numerous immunoreactive neurons were demonstrated in the protocerebrum (exclusive of optic lobes) and suboesophageal ganglion where 20 and 15 symmetrical clusters of reactive cells, respectively, were observed. Immunoreactive cells also occurred in the tritocerebrum, the optic lobes and the frontal ganglion. In the corpora cardiaca, gastrin/CCK-like material was found both within intrinsic cells and axon terminals. RIA measurements support the immunohistochemical results in so far as large amounts of gastrin/CCK-like material were detected in the brain, corpora cardiaca and suboesophageal ganglion complex. Both boiling water-acetic acid- and methanol-extraction procedures were performed. Comparisons of the results lead to the conclusion that a large part of the gastrin/CCK-like material occurs as small molecules. Immunohistochemical procedures performed on material fixed in a solution of picric acid-paraformaldehyde demonstrated differences in the immunoreactivity of the tested antisera. First, the immunohistochemical reaction was always more pronounced when the CCK-8NS antiserum was used instead of the CCK-8S antiserum, which may be interpreted by a lower affinity of the latter. In the second place, some neurons strongly stained by the CCK-8NS antiserum were only very faintly if at all stained by the CCK-8S antiserum, which may mean that different peptides or at least distinct forms of the same precursor are detected.
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    Springer
    Cell & tissue research 254 (1988), S. 75-81 
    ISSN: 1432-0878
    Keywords: Cholecystokinin-like peptide ; Midgut ; Colloidal gold immunostaining ; Endocrine cells ; Aeschna cyanea ; Locusta migratoria ; Carausius morosus ; Periplaneta americana (Insecta)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Electron-microscopic immunocytochemistry for the demonstration of CCK-like material in basal endocrine cells of the midgut of Aeschna cyanea, Locusta migratoria, Carausius morosus and Periplaneta americana was performed by use of the peroxidase-antiperoxidase procedure and the colloidal gold method. Immunoreactive cells appeared scattered among digestive and regenerative cells of the epithelium. Immunoreactivity was specifically detected over round to oval electron-dense granules whose size appeared rather different from species to species. Thus, the average size of 30% (d30) of the largest granules ranged from 312 nm in Periplaneta americana to 159 nm in Carausius morosus with intermediate values in Aeschna cyanea (d30=195 nm) and Locusta migratoria (d30=225 nm).
    Type of Medium: Electronic Resource
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  • 5
    ISSN: 0749-503X
    Keywords: α-amylase ; LKA1 ; Lipomyces kononenkoae ; Saccharomyces cerevisiae ; Life Sciences ; Life Sciences (general)
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The expression in Saccharomyces cerevisiae and Schizosaccharomyces pombe of a cDNA copy of the Lipomyces kononenkoae IGC4052B α-amylase gene (LKA1), linked to the phosphoglycerate kinase gene (PGK1) promoter, resulted in the extracellular production of biologically active α-amylase (LKA1). However, transformation of S. cerevisiae and Schiz. pombe with a cosmid clone containing the complete genomic copy of LKA1, expressed from its native promoter, did not result in secretion of active α-amylase by any of the transformants. When the cDNA copy of LKA1 was expressed in S. cerevisiae under control of the wild-type L. kononenkoae promoter, biologically active α-amylase was secreted into the culture medium, indicating the recognition of the LKA1 promoter in S. cerevisiae. Sequence analysis of the GC-rich LKA1 promoter revealed canonical sequences that are homologous to the TATAAA, CAAT and CCAAT boxes and GCN4-binding sites that are present in several promoter sequences of S. cerevisiae. Primer extension analysis of LKA1 transcripts in L. kononenkoae indicated major initiation sites at nucleotides -64 and -65. S. cerevisiae and Schiz. pombe cells transformed with a plasmid containing the open reading frame of the genomic copy of LKA1, linked to the PGK1 promoter, did not produce α-amylase. Polymerase chain reaction mapping and sequence analysis revealed the presence of a 61-bp intron in the genomic copy of LKA1 that impaired synthesis of biologically active α-amylase in S. cerevisiae and Schiz. pombe. This intron contains donor, acceptor and branch sequences that correlate with the consensus sequences identified in the introns of split genes from Schiz. pombe and mammals. Pulsed-field gradient gel electrophoresis resolved at least eight chromosomal DNAs for L. kononenkoae IGC4052B and chromoblot analysis indicated that LKA1 is located on the second smallest chromosome, designated chromosome II.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
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