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  • amine oxidase  (2)
  • 21.60.Ev  (1)
  • 1990-1994  (3)
  • 1
    ISSN: 1434-601X
    Keywords: 21.60.Ev ; 27.90.+b
    Source: Springer Online Journal Archives 1860-2000
    Topics: Physics
    Notes: Abstract Positive and negative parity bands have been followed up to 10+ (possibly 12+) and 11− in224Ra and are compared to the corresponding bands in the isotone226Th. If a constant value of the intrinsic quadrupole moment is assumed for allE2 transitions in224Ra theE1/E2 branching ratios are consistent with an intrinsic dipole moment of ¦Q1¦=0.032(3)e·fm. This small value, as compared to ¦Q1¦=0.30(2)e·fm for226Th, can be explained by an almost complete cancellation of large positive liquid-drop and negative shell-model contributions.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 0749-503X
    Keywords: Hansenula polymorpha ; alcohol oxidase ; amine oxidase ; choline ; peroxisome-deficient mutant ; enzyme assembly ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: We have studied the expression of alcohol oxidase (AO) in a peroxisome-deficient mutant strain of Hansenula polymorpha. High levels of octameric, active AO (up to 3·0 U/mg protein) were detected in cells grown at low dilution rates in a glucose-limited chemostat in the presence of choline as the sole nitrogen source. Monomeric or other intermediate forms of AO were not detected in the mutant strain. This indicated that assembly of the protein into active octameric molecules in the cytosol was as efficient as in wild-type cells where this process is confined to the peroxisomal matrix. At relatively low rates of expression (less than 1 U/mg protein) AO was localized throughout the cytosol and, surprisingly, was also present inside the nucleus. However, at enhanced levels large crystalloids were formed. Generally one crystalloid was observed per cell, whereas smaller ones were occasionally found in developing buds. Also large crystalloids have been observed inside the nucleus. These crystalloids were not surrounded by a membrane. Based on the morphology of the molecules that constituted these crystalloids and the results of (immuno)cytochemical experiments we conclude that the crystalloids are composed of octameric AO molecules, arranged in a regular lattice, identical to the 3-dimensional architecture previously described for the crystalline matrix of peroxisomes in methanol-grown wild type cells of H. polymorpha. Attempts to purify the crystalloids by conventional fractionation methods failed, due to their apparent fragility; however, (immuno)cytochemical experiments revealed that catalase and dihydroxyacetone synthase were also associated with these structures.
    Additional Material: 15 Ill.
    Type of Medium: Electronic Resource
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  • 3
    ISSN: 0749-503X
    Keywords: Hansenula polymorpha ; peroxisomes ; amine oxidase ; peroxisomal targeting signal ; homologous recombination ; integration ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Amine oxidase (AMO) is a peroxisomal matrix protein of Hansenula polymorpha, which is induced during growth of the yeast in media containing primary amines as a sole nitrogen source. The deduced amino acid sequence of the protein contains an SRL sequence at nine amino acids from the C-terminus. In this study, we have examined the possible role of the SRL motif in sorting of AMO to peroxisomes by mutating the corresponding gene sequence. For this purpose, we have developed a DNA construct that is specifically integrated into the AMO locus of the H. polymorpha genome, placing the mutant gene under the control of the endogenous AMO promoter and eliminating expression of the wild-type gene. Analysis of a stable transformant, containing the desired gene configuration, showed that mutation of the C-terminal sequence neither interfered with correct targeting of the protein into the peroxisome nor displayed significant effects on its activity. From this, it was concluded that the SRL-containing C-terminus is not essential for peroxisomal targeting of AMO in H. polymorpha.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
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