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PITUITARY HORMONE PURIFIC… - Göteborgs universitet Till startsida
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Konferensbidrag (offentliggjort, men ej förlagsutgivet)
Författare Ingibjörg Einarsdottir
L. Anjos
Jon Hildahl
Björn Thrandur Björnsson
DM Power
Publicerad i 7th International Congress on the Biology of Fishes, Book of Abstracts
Publiceringsår 2006
Publicerad vid Zoologiska institutionen
Språk en
Ämneskategorier Biologiska vetenskaper


Widely used methods for peptide hormone purification, such as gel filtration chromatography combined with rpHPLC, are time-consuming and often give low yields and instable proteins. The Model 491 Prep Cell from Bio-Rad provides a continuous-elution electrophoresis technique to separate proteins. The protein mixture runs through a cylindrical gel, proteins are separated by size and charge, as they elute from the matrix and are collected using a fraction collector. Sub-samples are assessed by SDS-PAGE and protein identity is verified by Western blot analysis. We applied this technique to separate putative hormones from adult Atlantic halibut pituitaries. Soluble proteins from homogenized pituitaries were denatured and subjected to continuous-elution electrophoresis. The fractions sampled contained purified proteins with molecular sizes ranging from 10 to 33 kDa. Fractions containing proteins with molecular weights of approximately 21, 24, 28 and 32 kDa were identified as putative growth hormone, prolactin, somatolactin and gonadotropins. These were analyzed further by mass spectrometry (MS) and identified with peptide mass protein fingerprinting. Good yield of highly purified GH was obtained, identified, and found to be biologically stable. Subsequently, it was used for radioactive labeling and as standards in a homologous RIA. Using this assay, the GH was measured in halibut larvae from start-feeding through metamorphosis, showing a stable size-related GH content of the head region. Funded by the EU.

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