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  • waxy protein  (3)
  • granule-bound starch synthase  (2)
  • Cavernous sinus  (1)
  • 1
    Electronic Resource
    Electronic Resource
    Follow-up MRI in dural arteriovenous malformations involving the cavernous sinus: emphasis on detection of venous thrombosis (1992)
    Springer
    Neuroradiology 34 (1992), S. 423-427 
    Details
    ISSN: 1432-1920
    Keywords: Dural arteriovenous malformations ; Cavernous sinus ; Venous thrombosis ; Magnetic resonance imaging ; Magnetic resonance angiography
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Six patients with a dural arteriovenous malformation (dural AVM) involving the cavernous sinus were followed up with magnetic resonance imaging in order to assess change in the lesions. Spin-echo (SE) imaging of three patients in whom the AVM appeared to have closed at least 1 month earlier (two of them spontaneously, and one after external carotid artery embolization) showed neither apparent flow void in the involved cavernous sinus nor evidence of venous thrombosis. SE images of the other three patients who had not been cured by external carotid artery embolization (two of whom were examined within a week of treatment), detected persisting arteriovenous shunts, including high-flow cortical venous drainage, seen as flow void. Two-dimensional time-of-flight MR angiography (2D TOF MRA) was performed simultaneously in three patients. Whereas shunting blood and the normal cavernous sinus were of high intensity, presumed thrombosed cavernous sinuses were isointense with stationary brain tissue. SE imaging can confirm the resolution of arteriovenous shunts, but poorly delineates ver acute and chronic thrombosis of the draining veins. In contrast, 2D TOF MRA directly demonstrates flowing blood, permitting the diagnosis of venous thrombosis; it should be included in follow-up of a dural AVM involving the cavernous sinus when venous thrombosis is suspected.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00596507
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Comparison of the primary structure ofwaxy proteins (granule-bound starch synthase) between polyploid wheats and related diploid species (1996)
    Springer
    Biochemical genetics 34 (1996), S. 403-413 
    Details
    ISSN: 1573-4927
    Keywords: polyploid wheat ; amino acid sequence ; waxy protein ; related diploid species
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract Thewaxy proteins encoded by the genomes A, B, and D in polyploid wheats and related diploid species were isolated by SDS-PAGE. The N-terminal amino acid sequences of mature proteins and V8 protease-induced fragments were determined. A total of five amino acid substitutions was detected in these sequences, which represent about 10% of the whole sequences of thewaxy proteins. A comparison of these sequences in polyploid wheats with those in related diploid species revealed the following: (i)waxy proteins encoded by the A genome of polyploid wheats were identical to that ofTriticum monococcum, (ii) thewaxy protein encoded by the B genome ofT. turgidum was identical to that ofT. searsii, but differed from those ofT. speltoides andT. longissimum by one amino acid substitution, (iii) thewaxy protein encoded by the B genome ofT. aestivum differed from that encoded by the B genome ofT. turgidum by one amino acid substitution, and (iv) thewaxy protein encoded by the D genome ofT. aestivum was identical to that ofT. tauschii.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00570121
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    Variation in the primary structure ofwaxy proteins (granule-bound starch synthase) in diploid cereals (1995)
    Springer
    Biochemical genetics 33 (1995), S. 269-281 
    Details
    ISSN: 1573-4927
    Keywords: diploid cereals ; waxy protein ; granule-bound starch synthase ; amino acid sequence
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract The molecular weights ofwaxy proteins, by SDS-PAGE, and the N-terminal amino acid sequences of mature protein and of V8 protease-induced fragments were determined in diploid cereals. The homology of the primary structure was relatively high among cereals examined here, and there appeared to be a common sequence, V-F-V-G-A-E-M-A, in the vicinity of the N terminus. Based on the amino acid sequences, these cereals could be divided into two groups, including corn and rice in one and diploid wheat, fourAegilops species, rye, and barley in the other. In diploid wheat andAegilops species there were substitutions of amino acids in the primary structure. Variations of this sort suggest that the primary structure ofwaxy proteins would provide clues to the phylogenetic relations in the wheat group.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00553625
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    Paper (German National Licenses)
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  • 4
    Electronic Resource
    Electronic Resource
    Variation in the primary structure ofwaxy proteins (granule-bound starch synthase) in diploid cereals (1995)
    Springer
    Biochemical genetics 33 (1995), S. 269-281 
    Details
    ISSN: 1573-4927
    Keywords: diploid cereals ; waxy protein ; granule-bound starch synthase ; amino acid sequence
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract The molecular weights ofwaxy proteins, by SDS-PAGE, and the N-terminal amino acid sequences of mature protein and of V8 protease-induced fragments were determined in diploid cereals. The homology of the primary structure was relatively high among cereals examined here, and there appeared to be a common sequence, V-F-V-G-A-E-M-A, in the vicinity of the N terminus. Based on the amino acid sequences, these cereals could be divided into two groups, including corn and rice in one and diploid wheat, fourAegilops species, rye, and barley in the other. In diploid wheat andAegilops species there were substitutions of amino acids in the primary structure. Variations of this sort suggest that the primary structure ofwaxy proteins would provide clues to the phylogenetic relations in the wheat group.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02401857
    Library Location Call Number Volume/Issue/Year Availability
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    Paper (German National Licenses)
    Fulltext
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