TY  - THES
AU  - Debowski, Katharina
TI  - Identifizierung und Charakterisierung eines neuen Bindeproteins für zyklische Nukleotide
VL  - 4260
IS  - Juel-4260
SN  - 0944-2952
PB  - Univ. Köln
VL  - Dr. (Univ.)
CY  - Jülich
M1  - PreJuSER-1297
M1  - Juel-4260
T2  - Berichte des Forschungszentrums Jülich
SP  - VII, 107 p
PY  - 2008
N1  - Record converted from VDB: 12.11.2012
N1  - Köln, Univ., Diss., 2007
AB  - Cyclic adenosine monophosphate (cAMP) and cyclic guanosine monophosphate are important intracellular messengers. Binding of cyclic nucleotides controls the activity of protein kinases, ion channels and guanine-nucleotide-exchange factors in many cells. The SCNBP (soluble cyclic nucleotide-binding protein) is a novel uncharacterized protein predicted to comprise a cyclic nucleotide-binding domain. This protein belongs to neither of the known families of effector proteins for cyclic nucleotides. Within 17 distinct species - from marine invertebrates to humans - genes orthologous to the mouse SCNBP are present. Hence, the SCNBP could belong to a novel class of effector proteins for cyclic nucleotides. Northern blot experiments with mouse tissue indicate that the mRNA of SCNBP is expressed predominantly in the testis and by means of in situ hybridization it was specifically detected in spermatocytes. In the present study, SCNBP expression has been analyzed in mouse testis utilizing specific antibodies. I could provide evidence that two distinct SCNBP variants are present in mouse testis. To approach the physiological function of SCNBP, I identified by immunoprecipitation and mass spectrometry proteins in mouse testis that potentially interact with SCNBP. For a comprehensive biochemical study, SCNBP was heterologously expressed in Chinese hamster ovary (CHO) cells. Following fermentation of these cells in a stirred tank bioreactor I purified SCNBP by affinity chromatography.
LB  - PUB:(DE-HGF)11 ; PUB:(DE-HGF)3
UR  - https://juser.fz-juelich.de/record/1297
ER  -