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  • 1
    Electronic Resource
    Electronic Resource
    Porcine amelogenins (1994)
    Springer
    Calcified tissue international 54 (1994), S. 69-75 
    Details
    ISSN: 1432-0827
    Keywords: Porcine secretory enamel ; Porcine amelogenin ; Plasma desorption mass spectometry ; Amino acid sequence ; CNBr cleavage
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine , Physics
    Notes: Abstract Amelogenins were extracted from the thin outer layer of porcine secretory enamel and purified by gel filtration and reverse-phase HPLC. The results of amino acid sequencing of the purified porcine amelogenins indicated the presence of at least four prototype amelogenins translated from alternatively spliced transcripts. The results of mass spectroscopy of the CNBr-cleaved peptides derived from the 25kDa amelogenin indicated that porcine 25kDa amelogenin is neither phosphorylated nor glycosylated.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00316293
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Enamelins in the newly formed bovine enamel (1993)
    Springer
    Calcified tissue international 53 (1993), S. 257-261 
    Details
    ISSN: 1432-0827
    Keywords: Bovine enamelin ; Amelogenin ; Newly formed enamel ; Western blot
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine , Physics
    Notes: Summary The possibility of using the antisera raised in rabbits against the porcine 25 kDa amelogenin, 32 and 89 kDa enamelins, and the 13–17 kDa nonamelogenin for the differentiation and identification of the protein components in bovine immature enamel was examined. Although the immunoreactivities of these antisera against bovine enamel proteins were weaker than those against the porcine proteins, it was found that these antisera could differentiate and demonstrate immunohistochemically a characteristic distribution of three different kinds of enamel protein components in the bovine secretory stage enamel similar to those observed in the porcine immature enamel. Of the several high molecular weight proteins being reactive to the anti-porcine 32 and 89 kDa enamelin sera, the 130 kDa protein, having the highest molecular weight, was extracted and purified from the bovine enamel sample which was obtained by peeling approximately 30-μm thickness of the outermost layer of the secretory stage enamel. The amino acid composition of the 130 kDa protein was similar to the known bovine enamelins, and was rich in aspartic acid, glutamic acid, proline, and glycine. The results could suggest that the enamelins of lower molecular weight than this protein, which are found in the bovine secretory stage enamel, are derived from this precursor protein.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01320911
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    Carbohydrate moieties of procine 32 kDa enamelin (1995)
    Springer
    Calcified tissue international 56 (1995), S. 323-330 
    Details
    ISSN: 1432-0827
    Keywords: Porcine secretory enamel ; Porcine 32 kDa enamelin ; Asparagine-linked oligosaccharide ; Pyridylamination ; Sequential exoglycosidase digestion
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine , Physics
    Notes: Abstract The structures of asparagine-linked oligosaccharides of porcine 32 kDa enamelin are reported. The oligosaccharides were released by N-oligosaccharide glycopeptidase digestion, and the reducing ends of the oligosaccharides were derivatized with a fluorescent reagent, 2-aminopyridine. The pyridylamino oligosaccharides were separated into eight kinds of oligosaccharides. The structures of these oligosaccharides were determined by a combination of a sequential exoglycosidase digestion and a two-dimensional suger mapping technique. The oligosaccharides consisted of fucose, galactose, mannose, N-acetylglucosamine, and N-acetylneuraminic acid, and were classified into two groups according to their core-sugar chain structures; one was a biantennary-type and the other was a triantennary-type oligosaccharide. The variation of the oligosaccharides in each of these groups was caused by the differences in the number, the site, and the mode of linkage of N-acetylneuraminic acid to the core-sugar chains.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00318054
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  • 4
    Electronic Resource
    Electronic Resource
    Immunochemical and immunohistochemical study of the 27- and 29-kDa calcium-binding proteins and related proteins in the porcine tooth germ (1997)
    Springer
    Histochemistry and cell biology 107 (1997), S. 485-494 
    Details
    ISSN: 1432-119X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract  Our previous report identified 27- and 29-kDa calcium-binding proteins in porcine immature dental enamel. In this study we revealed that the N-terminal amino acid sequences of the two proteins were identical: LLANPXGXIPNLARGPAGRSRGPPG. The sequence matches a portion of the amino acid sequence of the porcine sheath protein, sheathlin. Porcine tooth germs were investigated immunochemically and immunohistochemically using specific antibodies raised against synthetic peptide that included residues 13–25 of this sequence. The affinity-purified antibodies reacted with several proteins extracted from newly formed immature enamel in immunochemical analyses, especially protein bands migrating at 62, 35–45, 29, and 27 kDa in SDS-polyacrylamide gels. The largest protein detected was a weak band near 70 kDa. In immunochemical analyses of proteins extracted from the inner (old) immature enamel, the antibody reacted faintly with the 27- and 29-kDa proteins. In immunohistochemical preparations, the Golgi apparatus and secretory granules of the secretory ameloblast, and the surface layer of immature enamel showed immunoreactivity. The immunoreactivity of immature enamel just beneath the secretory face of the Tomes’ process was intense. No immunoreactivity was found in the Golgi apparatus of the maturation ameloblast. These results suggest that the 70-kDa protein, whose degradation might be very fast, is the parent protein of the 27- and 29-kDa proteins.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s004180050136
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  • 5
    Electronic Resource
    Electronic Resource
    Measurement of fetal movements using multichannel ultrasound pulsed Doppler: Autorecognition of fetal movements by maximum entropy method (1993)
    Springer
    Medical & biological engineering & computing 31 (1993), S. S59 
    Details
    ISSN: 1741-0444
    Keywords: Displacement estimation ; Fetal behaviour ; Fetal breathing movements ; Fetal monitoring ; Maximum entropy method ; Pulsed ultrasonic Doppler ; Signal processing
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Abstract Changes in fetal movements indicate biophysical conditions and functional development. The precise evaluation of fetal movements in clinical medicine requires the development of a continuous automated monitoring technique. A basic study of the measurement of fetal movements was carried out by modifying the Doppler ultrasound module of a cardiotocograph to produce low-frequency Doppler signals and five simultaneous outputs at various depths. These outputs represent displacement inside tissue at the various depths. Signal processing was executed on a 32-bit computer with a high-accuracy displacement estimation technique using the arctangent method. Results showed successful tracking of minute movements, such as fetal breathing movements (FBM), while rejecting other movements derived from maternal breathing etc. Using spectral analysis by the maximum entropy method (MEM), fetal movements were classified in three groups (FBM, fetal gross movements (FGM) and fetal heart movements (FHM)), based on the character of their special peak frequencies. The order of movement recognition was first FGM, then FBM and lastly FHM. FBM were more successfully recognised by MEM than by conventional B-mode observation methods. Small body movements were difficult to recognise as FGM by MEM in some cases. Although further studies are required for clinical application, it appears that automated assessments of fetal movements should be possible with this technique.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02446651
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    Paper (German National Licenses)
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