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Title:

Binding analysis of 1alpha- and 17alpha-dihydrotestosterone derivatives to homodimeric sex hormone-binding globulin.

Document type:
Journal Article; Article
Author(s):
Metzger, J; Schnitzbauer, A; Meyer, M; Söder, M; Cuilleron, CY; Hauptmann, H; Huber, E; Luppa, PB
Abstract:
Binding studies of the interaction of immobilized 1alpha- and 17alpha-aminoalkyl derivatives of 5alpha-dihydrotestosterone (DHT) with purified N-deglycosylated homodimeric human sex hormone-binding globulin (SHBG) were performed using a surface plasmon resonance biosensor. These 1alpha- and 17alpha-derivatives with spacers of appropriate lengths between the amine function and the steroid ring skeleton enabled privileged, sterically undisturbed, interactions of either the 17- or 3-characteristic...     »
Journal title abbreviation:
Biochemistry
Year:
2003
Journal volume:
42
Journal issue:
46
Pages contribution:
13735-45
Language:
eng
Fulltext / DOI:
doi:10.1021/bi035269k
Pubmed ID:
http://view.ncbi.nlm.nih.gov/pubmed/14622020
Print-ISSN:
0006-2960
TUM Institution:
Institut für Klinische Chemie und Pathobiochemie
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