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  • 1
    Electronic Resource
    Electronic Resource
    A 300 kilobase interval genetic map of rice including 883 expressed sequences (1994)
    [s.l.] : Nature Publishing Group
    Nature genetics 8 (1994), S. 365-372 
    Details
    ISSN: 1546-1718
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Medicine
    Notes: [Auszug] We have constructed a high resolution rice genetic map containing 1,383 DNA markers at an average interval of 300 kilobases (kb). The markers, distributed along 1,575 cM on 12 linkage groups, comprise 883 cDNAs, 265 genomic DNAs, 147 randomly amplified polymorphic DNAs (RAPD) and 88 other DNAs. ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/ng1294-365
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  • 2
    Electronic Resource
    Electronic Resource
    Affinity of bone sialoprotein and several other bone and dentin acidic proteins to collagen fibrils (1992)
    Springer
    Calcified tissue international 51 (1992), S. 438-442 
    Details
    ISSN: 1432-0827
    Keywords: Bone sialoprotein ; Phosphophoryn ; Bone Gla protein ; Bone proteoglycan ; Collagen binding
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine , Physics
    Notes: Summary Bone and dentin contain several kinds of mineral-binding proteins and cell-attachment proteins. The authors examined the affinity of these proteins to type I collagen, a major matrix protein of the tissue. Bone sialoprotein (BSP), bone Gla protein (BGP), bone small proteoglycan II (PG II), osteonectin (ON), and dentin phosphophoryn (DPP) were labeled with fluorescein isothiocyanate and incubated with reconstituted type I collagen fibril. DPP, BGP, BSP, and PG II were absorbed significantly to the collagen fibril at physiological ionic strength with dissociation constants of 10-6–10-7 M. BSP and PG II enhanced the fibrillogenesis of collagen. These acidic proteins can affect the surface properties of collagen fibril, and BSP, having the cell-attachment sequence Arg-Gly-Asp, possibly mediates interaction between collagen fibril and cells.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00296677
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  • 3
    Electronic Resource
    Electronic Resource
    Biochemical properties of collagen from ligaments and periarticular tendons of the human knee (1994)
    Springer
    Knee surgery, sports traumatology, arthroscopy 2 (1994), S. 229-233 
    Details
    ISSN: 1433-7347
    Keywords: Collagen ; Ligaments ; Periarticular tendons ; Human knee
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine , Sports Science
    Notes: Abstract The biochemical properties of collagens from the periarticular connective tissues of the human knee (ligaments, semitendinosus and gracilis tendons, and the iliotibial band) were investigated in subjects ranging from 20 to 70 years of age. Although the total collagen content of most tissues was more than 90% of the dry weight, the anterior cruciate ligament and the iliotibial band had relatively low collagen contents. There were no significant changes in the tissue collagen content with aging. However, the anterior cruciate ligament and the patellar tendon of the 20-year-old subject had a higher content of soluble collagen than the other ligaments and tendons. The iliotibial band of the 20-year-old subject contained more collagen that was soluble by a combination of salt, sodium citrate extractions and pepsin digestion. Dihydroxylysinonorleucine was the major reducible cross-link of collagen from all the ligaments. The amount of dihydroxylysinonorleucine in the anterior cruciate ligament of the 20-year-old subject was much higher than that in the other ligaments. In contrast, the tendons and the iliotibial band contained a large amount of histidino-hydroxymerodesmosine and hydroxylysinonorleucine, while the patellar tendon was the only tendon with a significant content of dihydroxylysinonorleucine. Hydroxypyridinium non-reducible cross-links were more abundant in collagens from ligaments than in collagens from the other tissues. The cross-link study and the analysis of collagen solubility showed that patellar tendon collagen more closely resembled the collagen from the anterior cruciate ligament than that from periarticular tendons. It was also shown that the anterior cruciate ligament contains relatively immature collagen compared with the other ligaments. Our findings may contribute to an improved understanding of the functions of the ligaments and tendons around the knee joint. In addition, the data may provide some useful pointers that will help in selection of periarticular tissues as appropriate substitutes for ligament replacement.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01845593
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    Paper (German National Licenses)
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