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  • Collagen  (4)
  • Springer  (4)
  • 2005-2009
  • 1980-1984  (4)
  • 1955-1959
  • 1980  (4)
Collection
Publisher
  • Springer  (4)
Years
  • 2005-2009
  • 1980-1984  (4)
  • 1955-1959
Year
  • 1
    ISSN: 1432-0827
    Keywords: Growth plate ; Dwarf ; Collagen ; Hexosamine
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine , Physics
    Notes: Summary This study was performed to compare the extractability of dwarf growth plate collagen and hexosamine with that of homozygous nonaffected Malamutes and to measure the activity of three of the enzymes involved in the post-translational modifications of the collagen molecule. No significant differences were found in the activity of prolyl hydroxylase or lysyl oxidase in the dwarf growth plates. Lysyl hydroxylase activity in the dwarf was decreased to 22% and 33% that of the activity present in the homozygous nonaffected growth plates. Amino acid analysis of the collagen isolated from dwarf growth plates failed to reveal any decrease in hydroxylysine content. Growth plates were extracted with either 1 M sodium chloride or 4 M guanidine hydrochloride. The extracts were applied to a DEAE-cellulose column. Amino acid analyses of the material which did not bind to DEAE revealed a slight decrease in the amount of guanidine-extractable hydroxyproline in the dwarf but a 60-fold increase in the amount of salt-extractable hydroxyproline in the dwarf growth plates. Material which eluted with 1 M sodium chloride was analyzed for hexosamine. There was a 10-fold increase in the amount of salt-extractable hexosamine present in the dwarf growth plates, whereas no significant differences were observed in the guanidine-extracted material. Hexosamine analysis of the growth plates revealed a significant increase in the total amount of hexosamine present in the dwarf growth plates. SDS-polyacrylamide gels of the material which did not bind to DEAE as well as the pepsin digested, 0.9M sodium chloride precipitated collagen demonstrated the presence of only type II collagen.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Calcified tissue international 31 (1980), S. 257-259 
    ISSN: 1432-0827
    Keywords: Piezoelectricity ; Collagen
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine , Physics
    Notes: Summary Tissue collagen exhibits several levels of structural organization, and this complicates efforts to determine the origin of its piezoelectricity. We made collagen films—by evaporation and electrodeposition from solution—and examined the relation between collagen's piezoelectricity and its electron microscopic appearance. We found that the electrodeposited films were more organized and exhibited higher piezoelectric coefficients than the evaporated films. Despite this, the evaporated films were piezoelectric, thereby suggesting that the effect originates either at the level of the tropocollagen molecule or, at most, with aggregated structures no larger than 50 Å in diameter.
    Type of Medium: Electronic Resource
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  • 3
    ISSN: 1432-0827
    Keywords: Diphosphonates ; Cartilage ; Collagen ; Erbium
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine , Physics
    Notes: Summary The bone-seeking agent99mTc-labeled 1-hydroxyethylidene-1,1-diphosphonic acid (HEDP) unexpectedly binds to particles of human articular cartilage as well as cortical bone in vitro. Collagen also sequesters this compound, suggesting that collagen contributes to the uptake of99mTc-HEDP by cartilage and bone. Particles of the bone mineral calcium hydroxyapatite also bind99mTc-HEDP in vitro. Pretreatment of particles with Er3+ stimulates binding in each case. Lowering the pH of incubation to pH 2 has this effect for bone, cartilage, and collagen, but not for calcium hydroxyapatite. Mechanisms additional to the simple ionic attraction between the phosphonate groups of HEDP and metal cations such as Ca2+ are responsible for the uptake of99mTc-HEDP by body tissues.
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    Springer
    Bulletin of experimental biology and medicine 90 (1980), S. 1707-1709 
    ISSN: 1573-8221
    Keywords: Collagen ; C1q component of complement ; nucleic acids
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Type of Medium: Electronic Resource
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