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  • Saccharomyces cerevisiae  (2)
  • 46L55  (1)
  • Capillary density  (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
    Electronic Resource
    Electronic Resource
    Springer
    Pflügers Archiv 375 (1978), S. 245-249 
    ISSN: 1432-2013
    Keywords: Human muscles ; Soleus ; Gastrocnemius ; Capillary density ; Capillary arrangement ; Fibre type area
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract 4 healthy men had biopsies taken from the soleus and the lateral head of the gastrocnemius muscle for determination of capillary supply, fibre type distribution and fibre area. In serial transverse sections slow twitch (ST) and fast twitch (FT) fibres were identified histochemically by myofibrillar adenosine triphosphatase stains and capillaries visualized by a periodic acid Schiff stain after digestion of glycogen by α-amylase. In soleus, ST and FT fibre type areas were approximately two times greater than in gastrocnemius. FT fibres (11060 μm2) were 50% greater than ST fibres (7520 μm2) in soleus, whereas no difference between FT and ST fibres was observed in gastrocnemius (4730 μm2 and 4310 μm2, respectively). Both muscles were mixed with respect to fibre types but in all subjects soleus had a higher relative content of ST fibres than gastrocnemius. The area occupied by ST fibres relative to total area was 64% in soleus and 50% in gastrocnemius. Capillary density was 288 capillaries·mm−2 in soleus and 365 in gastrocnemius. Evaluated on the basis of mean number of capillaries in contact with fibres of each type relative to fibre type area (μm−2·10−3) individual ST fibres had a richer capillary supply than FT fibres in both soleus (0.84 and 0.57, respectively) and gastrocnemius (1.12 and 0.92, respectively). Differences in organization of the capillary network between soleus and gastrocnemius were observed. Capillaries are running mainly parallel to the muscle fibres in gastrocnemius, but tortuously and/or frequently branching in soleus. Tortuously and/or frequently branching capillaries implies nutritional advantages, which will not be reflected in the quantitative data obtained from counts of capillaries made on transverse sectioned muscle. Therefore the absolute values given for soleus and gastrocnemius, respectively, cannot be directly compared.
    Type of Medium: Electronic Resource
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  • 3
    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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  • 4
    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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