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  • 1
    Electronic Resource
    Electronic Resource
    Interactions of benzodiazepines with human serum albumin (1973)
    Springer
    Naunyn-Schmiedeberg's archives of pharmacology 278 (1973), S. 301-312 
    Details
    ISSN: 1432-1912
    Keywords: Circular Dichroism ; Benzodiazepines ; Albumin-Binding ; Partition Coefficients
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary The circular dichroism spectra of 12 benzodiazepine derivatives studied in presence of human serum albumin are presented. Nearly all substances give biphasic extrinsic Cotton effects. At the CD maxima the molar ellipticities and the anisotropy factors are calculated. The influence of the chemical structure of the benzodiazepines on the induced Cotton effect is discussed. There is a linear correlation between the anisotropy factors and the logarithms of the partition coefficients of the substances. It is suggested that the phenyl ring of the benzodiazepine molecule is one of the essential groups for the binding of these substances to human serum albumin.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00500291
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  • 2
    Electronic Resource
    Electronic Resource
    Characterization of the binding of benzodiazepines to human serum albumin (1973)
    Springer
    Naunyn-Schmiedeberg's archives of pharmacology 280 (1973), S. 229-237 
    Details
    ISSN: 1432-1912
    Keywords: Benzodiazepines ; Albumin Binding ; Gel Filtration
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary The binding of eleven benzodiazepine derivatives to human serum albumin (HSA) was determined by means of sephadex gel filtration. The albumin binding of the substances was characterized by the percentage of bound drug, the binding constants k +, K 1 and m, the number of binding sites per albumin molecule, and the free binding energy. Under the conditions chosen in these experiments there seems to exist only one binding site of the same type for all investigated benzodiazepines at the HSA molecule. The affinities of the benzodiazepines to this binding site are very different. It is discussed which part of the benzodiazepine molecule represents the main binding group.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00501348
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  • 3
    Electronic Resource
    Electronic Resource
    Influence of pH on the benzodiazepine-human serum albumin complex (1974)
    Springer
    Naunyn-Schmiedeberg's archives of pharmacology 283 (1974), S. 67-82 
    Details
    ISSN: 1432-1912
    Keywords: Benzodiazepines ; Albumin Binding ; Circular Dichroism ; Gel Filtration ; pH Dependence
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary The influence of pH on the binding of benzodiazepine derivatives to HSA was studied by circular dichroism measurements and by gel filtration. The binding of nearly all benzodiazepines is increased by rising the pH from 6.60 to 8.20. For flurazepam, clonazepam, and nitrazepam this increase in binding is due to an increase of the affinities, while for the other substances the affinity remains constant and the number of binding sites is increased from one to two. The changes in binding of the benzodiazepines by rising the pH are explained by a cationic amino acid residue near or at the benzodiazepine binding site of the HSA molecule. This second binding site is not detectable by circular dichroism. For several of the substances rising the pH from 6.60 to 8.20, is accompanied by large alterations of the optical properties of the HSA-benzodiazepine complexes. These alterations are explained by changes of the asymmetric environment of the benzodiazepine binding site at the HSA molecule in the structural transition at slightly alkaline pH values. To explain the different reactions of the benzodiazepines within the N→B transition a theory is given.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00500146
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  • 4
    Electronic Resource
    Electronic Resource
    Benzodiazepines: Specific competitors for the binding of l-tryptophan to human serum albumin (1975)
    Springer
    Naunyn-Schmiedeberg's archives of pharmacology 288 (1975), S. 17-27 
    Details
    ISSN: 1432-1912
    Keywords: Human Serum Albumin Binding ; l-Tryptophan ; Displacing Agents ; Benzodiazepines
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary By means of the gel filtration technique, the effect of nine benzo-diazepine derivates on the binding of l-tryptophan to human serum albumin was investigated. Using equimolar tryptophan and benzodiazepine concentrations, all benzodiazepines with binding constants higher than 104 (M−1), displace l-tryptophan from its binding site to a high degree. The mechanism of the displacement was characterized as a competition for a common binding site. Some of the benzodiazepines displace l-tryptophan to a greater extent than salicylic acid. The benzodiazepines and tryptophan are the only substances known with a high degree of stereospecific binding to human serum albumin. This study shows that there is only one binding site on the human serum albumin molecule, which binds tryptophan and the benzodiazepines in a highly stereospecific manner. Therefore it is concluded that the benzodiazepines and l-tryptophan must have similarities in their molecular structure, so that both can bind to the common binding site in such specific manner. These considerations are discussed in regard to the known influence of benzodiazepine derivatives on the l-tryptophan metabolism in brain. A direct involvement of the reported displacement in the pharmacological actions of the drugs seems not to be relevant because of their small therapeutical plasma levels.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00501811
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  • 5
    Electronic Resource
    Electronic Resource
    Myelinated nerve cell perikaryon in mouse spinal cord (1972)
    Springer
    Cell & tissue research 128 (1972), S. 135-138 
    Details
    ISSN: 1432-0878
    Keywords: Spinal cord ; Mouse ; Myelinated neuronal soma ; Electron microscopy
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Description / Table of Contents: Zusammenfassung Im Thorakalmark (Hinterhornbereich) einer Wildmaus wurde ein kleines Nervenzellperikaryon beobachtet, das vollständig von einer Markscheide umhüllt war. Die Zahl der Markscheidenlamellen variierte zwischen 7 und 12. An einer Stelle konnte ein sogenanntes inneres Mesoperikaryon nachgewiesen werden. Die Bedeutung dieses zufällig erhobenen Befundes ist vorerst noch offen.
    Notes: Summary In the thoracic cord (posterior horn region) of a wild mouse, we have observed a small nerve cell soma completely enveloped by a myelin sheath. The number of myelin lamellae varied between 7 and 12. In one place, the existence of an inner ‘mesoperikaryon’ could also be shown. The significance of this fortuitous finding has not yet been explained.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00306893
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  • 6
    Electronic Resource
    Electronic Resource
    Uteroglobin-like antigen in the male genital tract secretions (1975)
    Springer
    Cell & tissue research 165 (1975), S. 1-11 
    Details
    ISSN: 1432-0878
    Keywords: Rabbit seminal vesicle ; Rabbit seminal plasma ; Genital tract secretion proteins ; Electron microscopy ; Disc electrophoresis ; Immunoelectrophoresis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary The secretion of the rabbit seminal vesicle has been investigated by morphological and biochemical means. Apical regions of seminal vesicle epithelial cells show highly active protein synthesizing and releasing organells. The secretory proteins released are analysed by disc-electrophoresis and three different immunological procedures. There is evidence for the presence of an uteroglobin-like antigen in seminal vesicle secretion. Comparison with seminal plasma indicates that the uteroglobin-like protein is also present in this fluid. The immunological and electrophoretical identity of rabbit uteroglobin, obtained from the uterus, with “male uteroglobin” is obvious, but molecular-biochemical and biological identity awaits further clarification. The demonstration of uteroglobin-like antigen in the male as in the female points towards new aspects in reproductive and contraceptive research.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00222795
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  • 7
    Electronic Resource
    Electronic Resource
    Recurrent amyloid tumor of the parotid gland (1995)
    Springer
    European archives of oto-rhino-laryngology and head & neck 252 (1995), S. 53-56 
    Details
    ISSN: 1434-4726
    Keywords: Parotid gland ; Amyloidosis ; Electron microscopy
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract A case of an organ-limited amyloid tumor of the left parotid gland is described with a history of recurrence. A slowly growing parotid mass was the only symptom. After 5.5 years following local excision, the patient was readmitted with a slowly growing recurrence in the superficial lobe of the previously treated gland. Lateral parotidectomy was performed with wide excision of the infiltrated tissue and preservation of the facial nerve. Primary amyloidosis of the AL type was confirmed with immunohistochemical studies revealing staining for lambda but not kappa light chains of immunoglobulins. There has been no clinical or laboratory evidence of systemic amyloidosis or recurrence after 2 years. To the best of our knowledge, this is the first report of a recurrent amyloid tumor of the parotid gland.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00171441
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