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  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Amino acids 3 (1992), S. 287-292 
    ISSN: 1438-2199
    Keywords: Amino acids ; Elastin ; Cross-link ; Connective tissue ; Marfan's syndrome ; Aneurysm
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Biochemical pathogenesis of the aortic connective tissue diseases (such as, Marfan's syndrome, dissecting aneurysm or aortic aneurysm) was examined by estimating glycoprotein, collagen and elastin contents in the aorta and the intramolecular cross-linking component (isodesmosine) and the intermolecular cross-linking components (cystine, histidinoalanine) in comparison with the control samples obtained from subjects with aortic regurgitation. The elastin content in the aorta and isodesmosine content obtained from the extract of the aortic sample found to be decreased. Ratio of cysteine residues (Cys/Cys-Cys) in the elastin fraction in disease increased. Content of histidinoalanine was found to be decreased. It may be suggested that elastin is maintained in its native nature and shape by intra- and inter-molecular cross-linking bridges, and they are readily denatured by various disease conditions. After elastin was solubilized by elastase, immunoreactive elastin content in those aortic diseases was found to be increased in the human connective tissue. Serum elastase and elastase-like activities tend to increase more than those in the control. These findings may suggest that the change in the structure of elastin would make more susceptible to elastase and other proteolytic enzymes. The reasonable hypothesis may be that molecular defect of fibillin or other constitutional structural glycoproteins produce deficient and functionally incompetent elastin associated microfibrils, and the defect of microfibrils cause to insufficient intra- and inter-molecular cross-links in elastin.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Amino acids 2 (1992), S. 289-296 
    ISSN: 1438-2199
    Keywords: Amino acids ; C-terminal peptide ; Thiohydantoin derivatives ; C-terminal sequencing ; Solid phase peptide sequencing
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary C-terminal amino acid sequence analysis seemed to be established procedure, as the counterpart of Edman's N-terminal sequencing method. However, poor recovery of the C-terminal amino acids in the reaction in homogeneous solution suggested further improvement of the method. In the present study, N-terminal amino acid was fixed covalently to the controlled pore glass (CPG) beads and the C-terminal amino acid was activated (by treating with acetic anhydride), coupled with thiocyanate to form thiohydantoin (TH) ring at the C-terminus. Then, the C-terminal amino acid was split off as the corresponding TH derivative, and analyzed by HPLC. Hydrolysis of the TH derivative was achieved at 60°C in the presence of 2 M HC1 for 2 h. Solid phase fixed peptide was washed simply with acetone, and dried for the next cycle of the reaction. So far obtained results in the heterogeneous mixture are not satisfactory in terms of the recovery of the C-terminal TH, and improvement of the recovery and further steps are under progress.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
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