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  • 1
    Electronic Resource
    Electronic Resource
    Serotonin-immunoreactive cells of peculiar shape in the urethral epithelium of the human penis (1987)
    Springer
    Cell & tissue research 249 (1987), S. 51-56 
    Details
    ISSN: 1432-0878
    Keywords: Penis ; Urethra ; Serotonin-immunoreactive cells ; Immunohistochemistry ; Human
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary The present study deals with endocrine-like cells in the urethra of human penis. A large number of basal-granulated cells immunoreactive for serotonin were dispersed in the urethral epithelium. No cellular elements were stained positively with antisera against bioactive peptides. The serotonin-immunoreactive cells consisted of a small oval perikaryon and slender processes, and resembled neurons in shape. An apical process reached the urethral lumen. The basal processes frequently branched out in a dendritic fashion, some running laterally for a considerable distance. The number of cells immunoreactive for serotonin was remarkably reduced in subjects over 60 years of age.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00215417
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Structural analysis of protein variants by mass spectrometry: Characterization of haemoglobin providence using a grand-scale mass spectrometer (1989)
    Chichester : Wiley-Blackwell
    Biological Mass Spectrometry 18 (1989), S. 563-565 
    Details
    ISSN: 0887-6134
    Keywords: Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: A grand-scale mass spectrometer with high mass resolution and high transmission was employed for the analysis of haemoglobin variant. Two variants were isolated from a haemolysate by chromatography. Secondary ion mass spectrometry of complex peptide mixtures derived from these variants precisely determined the molecular weight of abnormal peptides. The molecular weight, 2857.4 and 2858.4, indicated the amino acid substitutions of asparagine and aspartic acid, respectively, for lysine at position 82 of β globin chain. The mutations had been reported in haemoglobin Providence.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bms.1200180809
    Library Location Call Number Volume/Issue/Year Availability
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    Paper (German National Licenses)
    Fulltext
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