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  • Collagen  (6)
  • Springer  (6)
  • Cambridge University Press
  • International Union of Crystallography (IUCr)
  • Wiley
  • 1980-1984  (6)
  • 1940-1944
  • 1981  (2)
  • 1980  (4)
  • 1942
Collection
Keywords
Publisher
  • Springer  (6)
  • Cambridge University Press
  • International Union of Crystallography (IUCr)
  • Wiley
Years
  • 1980-1984  (6)
  • 1940-1944
Year
  • 1981  (2)
  • 1980  (4)
  • 1942
  • 1982  (1)
  • 1
    Electronic Resource
    Electronic Resource
    Studies of the intercellular matrix of growth plates from dwarf and homozygous nonaffected alaskan malamutes: Collagen and hexosamine (1980)
    Springer
    Calcified tissue international 32 (1980), S. 237-245 
    Details
    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
    URL: http://dx.doi.org/10.1007/BF02408547
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  • 2
    Electronic Resource
    Electronic Resource
    Studies on extractable and resistant proteoglycans from metaphyseal and cortical bone and cartilage (1981)
    Springer
    Calcified tissue international 33 (1981), S. 89-99 
    Details
    ISSN: 1432-0827
    Keywords: Soluble proteoglycans ; Resistant proteoglycans ; Collagen ; Bone ; Cartilage
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine , Physics
    Notes: Summary Soluble proteoglycans (SPG) were extracted from bovine (BCC) and human (HCC) costal cartilages by the dissociative method using 4 M guanidinium chloride (GuHCl). Proteoglycans which are resistant to extraction (RPG) were obtained following collagenase digestion or hydroxylamine treatment of the cartilage residues. Similarly, SPG were extracted from bovine metaphyseal and cortical bone using EDTA. The RPG were extracted from the bones using hydroxylamine. Density gradient fractionation under dissociative conditions of cartilage SPG and RPG followed by chromatography on Sepharose 2B revealed that A1D1 RPG are smaller than the SPG. SPG reacted with either collagenase or hydroxylamine are also smaller than the parent SPG. A1D1 fractions obtained from BCC-SPG and RPG or from mixtures of SPG and acid-soluble collagen are free of hydroxyproline. Hydroxyproline is not completely separated from HCC-RPG. Density gradient fractionation of bone proteoglycans and Sepharose chromatography of the A1 and A1D1 fractions showed that those obtained from metaphysis are larger than those from cortical bone. This was attributed to the presence of calcified cartilage in metaphyseal bone. The A1D1 fractions of the metaphyseal proteoglycans seemed to undergo self-association since this fraction is larger than the A1 fraction from which it is derived. Cortical bone proteoglycans do not behave similarly. Density gradient purification under dissociative conditions failed to separate hydroxyproline from the proteoglycans obtained from bone. It is hypothesized that in bone proteoglycans and collagen might be linked.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02409419
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  • 3
    Electronic Resource
    Electronic Resource
    Piezoelectricity in collagen films (1980)
    Springer
    Calcified tissue international 31 (1980), S. 257-259 
    Details
    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
    URL: http://dx.doi.org/10.1007/BF02407190
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  • 4
    Electronic Resource
    Electronic Resource
    Binding of the bone-seeking agent99mTc-1-hydroxyethylidene-1,1-diphosphonic acid to cartilage and collagen in vitro and its stimulation by Er3+ and low pH (1980)
    Springer
    Calcified tissue international 32 (1980), S. 91-94 
    Details
    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
    URL: http://dx.doi.org/10.1007/BF02408527
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  • 5
    Electronic Resource
    Electronic Resource
    Density of a sample bovine cortical bone matrix and its solid constituent in various media (1981)
    Springer
    Calcified tissue international 33 (1981), S. 499-504 
    Details
    ISSN: 1432-0827
    Keywords: Bone ; Collagen ; Density
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine , Physics
    Notes: Summary The density of a bovine cortical bone matrix sample was found in water, several ethanol-water solutions, and in the dried state. Previously the density of the same mineralized bone was found fresh and when desiccated. The volume in each state was estimated from the dimensional changes axially, tangentially, and radially. Confirmation was found by determining the density of dried specimens upon immersion in xylene. The amount of imbibed xylene provided an estimate of the free pore volume in the dried matrix. The volume fraction of the solid constituent, S, in the wet matrix was found to be 0.57, from which the density of S in various solutions was calculated. Density of wet matrix in 0.15 M saline: 1.180 g/cc; for dried matrix, 1.246 g/cc. Density of wet S in saline: 1.33 g/cc; for dried S, 1.42 g/cc, which matches published values for collagen molecules. Dimensional changes between wet and dried state of matrix match published values for artificially cross-linked rat tail tendon fibers. Axially: 1.04, by area: 2.27; by volume: 2.62. Estimate of intrafibrillar volume, assuming 80% of mineral is within fibrils: 0.73 cc/g dry collagen.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02409480
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  • 6
    Electronic Resource
    Electronic Resource
    Interaction of the C1q component of complement and collagen with nucleic acids and polyanions (1980)
    Springer
    Bulletin of experimental biology and medicine 90 (1980), S. 1707-1709 
    Details
    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
    URL: http://dx.doi.org/10.1007/BF00830455
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