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  • 1
    Electronic Resource
    Electronic Resource
    Spiro [3.5] nonane1 (1953)
    s.l. : American Chemical Society
    Journal of the American Chemical Society 75 (1953), S. 6228-6230 
    Details
    ISSN: 1520-5126
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/ja01120a035
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  • 2
    Electronic Resource
    Electronic Resource
    Correlative morphometric and biochemical analysis of purified extracellular matrix vesicles from rat alveolar bone (1983)
    Springer
    Calcified tissue international 35 (1983), S. 320-326 
    Details
    ISSN: 1432-0827
    Keywords: Extracellular matrix vesicles ; Vesicular fractional area ; Morphometric ; Purification
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine , Physics
    Notes: Summary Extracellular matrix vesicles were isolated from rat alveolar bone and purified by either gel filtration or discontinuous sucrose density gradient. Morphometric evaluation of electronmicrographs of pellets of purified and nonpurified vesicle fractions was correlated with the acitvity of vesicular enzymes. A high correlation was found between the percentage of area occupied by vesicles with electron-dense content (electron-dense vesicle fractional area) and the enzymatic activity. Highest enzymatic specific activities and electrondense vesicle fractional area were recorded in the “light” vesicle-enriched fraction obtained after equilibrium density centrifugation. These parameters revealed lowest values in the “heavy” vesicle-enriched fraction resolved by the same methods. The combined electron-dense and electron-lucent fractional area (vesicular fractional area) was similar in the different purified fractions. It is therefore suggested that the fraction obtained by gel filtration contains both “light” and “heavy” vesicles. Morphometric study is proposed as an additional criterion for the degree of purification of matrix vesicle preparations.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02405053
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  • 3
    Electronic Resource
    Electronic Resource
    Neutral peptidase activities in matrix vesicles from bovine fetal alveolar bone and dog osteosarcoma (1983)
    Springer
    Calcified tissue international 35 (1983), S. 791-797 
    Details
    ISSN: 1432-0827
    Keywords: Bone ; Osteosarcoma ; Matrix vesicles ; Alkaline phosphatase ; Aminopeptidase ; Naphthylamidase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine , Physics
    Notes: Summary Extracellular matrix vesicles from bovine fetal alveolar bone and from a dog osteosarcoma were isolated by differential centrifugation and then fractionated on a discontinuous sucrose density gradient. The fractions were examined by electron microscopy and were analyzed for protein, alkaline phosphatase, aminotripeptidase, and four different β-naphthylamidase activities. The low-density peak of enzyme activities was shown by electron microscopy to be much more homogeneous than the crude matrix vesicle fraction. Two major peaks of protein and enzyme activities were present, one in the high and one in the low density layers. There was good correlation between the activities of alkaline phosphatase and the various peptidases in the fractions from the sucrose density gradient. These results indicate a coexistence of peptidase and alkaline phosphatase in matrix vesicles. On the other hand, there was generally no correlation between the peptidase and alkaline phosphatase activities in vesicular specimens from bovine liver obtained in the same way. Most of the peptidase activity and about half of the alkaline phosphatase activity were solubilized from bone matrix vesicles by detergents. The extracted alkaline phosphatase and alanyl β-naphthylamidase activities were separated from each other on a DEAE-cellulose column.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02405125
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  • 4
    Electronic Resource
    Electronic Resource
    Racemization of aspartic acid in the extracellular matrix proteins of primary and secondary dentin (1993)
    Springer
    Calcified tissue international 53 (1993), S. 103-110 
    Details
    ISSN: 1432-0827
    Keywords: Dentin ; Extracellular proteins ; Racemization ; Aging
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine , Physics
    Notes: Summary The accumulation with age ofd-aspartic acid in primary and secondary human dentin was determined. In primary dentin, the plot of thed/l Asp ratio vs. age was found to fit first-order kinetics in accordance with the literature. But the secondary dentin behaved in an irregular manner and showed, in the great majority of cases, significantly increasedd/l Asp ratios. Possible reasons for these findings, such as differences in protein composition and/or in the prevailing temperature, are discussed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01321887
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  • 5
    Electronic Resource
    Electronic Resource
    Occurrence of actin-like protein in extracellular matrix vesicles (1982)
    Springer
    Calcified tissue international 34 (1982), S. 376-381 
    Details
    ISSN: 1432-0827
    Keywords: Matrix vesicles ; Bone ; Actin ; Rat
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine , Physics
    Notes: Summary Preliminary indications of the occurrence of actin and myosin in crude matrix vesicle preparations have been reported previously. In the present study extracellular matrix vesicles from rat alveolar bone were isolated. They were further purified by a sucrose density gradient. SDS-polyacrylamide gel electrophoresis of the purified vesicles revealed the presence of a polypeptide with a molecular weight of 43 K daltons and with electrophoretic mobility identical to that of blood platelet actin. The limited proteolysis of both 43 K dalton vesicular polypeptide and actin byStaphylococcus aureus-V8-protease revealed three fragments with identical electrophoretic mobility. In addition, the vesicular preparations inhibited the activity of DNase I, a property typical of actin monomers. Filamentous material extracted from matrix vesicles showed ultrastructural features of F-actin. Reaction of this material with heavy meromyosin resulted in arrowhead formation, which is characteristic of acto-heavy meromyosin. The occurrence of actin in extracellular matrix vesicles may account for their budding from the osteoblastic plasma membrane, their possible motility in the matrix, and maintenance of the spherical shape.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02411271
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  • 6
    Electronic Resource
    Electronic Resource
    Threshold Differentiation of Drive and Reward in the Olds Effect (1962)
    [s.l.] : Nature Publishing Group
    Nature 196 (1962), S. 699-700 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Fig. 1. Hesults of preliminary experiment on one animal. Crosses show the number of lever presses to extinction in successive 30-sec periods of normal extinction. Circles represent the number of lever presses in 30 sec of extinction during which a low intensity of repetitive stimulation was given, ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/196699a0
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  • 7
    Electronic Resource
    Electronic Resource
    Negative energy radiation and the second law of thermodynamics
    Amsterdam : Elsevier
    Physics Letters B 119 (1982), S. 72-74 
    Details
    ISSN: 0370-2693
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Physics
    Type of Medium: Electronic Resource
    URL: http://linkinghub.elsevier.com/retrieve/pii/0370-2693(82)90246-5
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  • 8
    Electronic Resource
    Electronic Resource
    Production of a monoclonal antibody against human amelogenin (1994)
    Springer
    Calcified tissue international 54 (1994), S. 76-80 
    Details
    ISSN: 1432-0827
    Keywords: Monoclonal antibody ; Human ; Amelogenin
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine , Physics
    Notes: Abstract The extracellular organic matrix of developing human enamel is composed of two major classes of proteins, the hydrophobic amelogenins and the acidic enamelins. In order to identify, purify, and characterize the amelogenins from this complex mixture of proteins, and to study their ultrastructural localization and their pathways of synthesis, secretion, and degradation, specific and sensitive probes are needed. In the present paper the production of a monoclonal antibody against human amelogenin employing an intrasplenic primary immunization protocol is described. The monoclonal antibody produced is IgM and recognizes major human amelogenin protein bands in Western immunoblot assays. It also recognizes amelogenin protein bands from other species, specifically bovine and porcine. Indirect immunohistochemical studies showed the monoclonal antibody to react specifically with the extracellular matrix of human developing enamel. It did not react with the underlying dentin layer.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00316294
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  • 9
    Electronic Resource
    Electronic Resource
    Erwiderung zur vorstehenden Bemerkung des Herrn Dr. Kolthoff (1927)
    Springer
    Colloid & polymer science 43 (1927), S. 52-52 
    Details
    ISSN: 1435-1536
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology , Mechanical Engineering, Materials Science, Production Engineering, Mining and Metallurgy, Traffic Engineering, Precision Mechanics
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01451561
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  • 10
    Electronic Resource
    Electronic Resource
    Ueber die lyotropen Eigenschaften des Nitrit-Ions (1928)
    Springer
    Colloid & polymer science 46 (1928), S. 22-23 
    Details
    ISSN: 1435-1536
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology , Mechanical Engineering, Materials Science, Production Engineering, Mining and Metallurgy, Traffic Engineering, Precision Mechanics
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01423667
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