Abstract:
:For evaluation whether the membrane fatty acid-binding protein is related to mGOT, studies on the structure and function of both purified proteins were performed. Physicochemical characterization revealed that both proteins are different: the membrane fatty acid-binding protein has a molecular weight of 40 kD and a pI of 8.5-9.0, whereas rat mGOT has a molecular weight of 44 kD and a pI of 9.5-10.0. According to this distinct differences, they migrated separately on 2-dimensional electrophoresis. Furthermore, monospecific antibodies against the membrane fatty acid binding protein did not react with rat mGOT. In co-chromatography studies only the membrane fatty acid-binding protein showed affinity for long chain fatty acids, but not mGOT. Moreover, membrane binding studies were performed with the monospecific antibody to the membrane fatty acid binding protein. The inhibitory effect of this antibody on plasma membrane binding of oleate was reversed after preabsorption of the antibody with the membrane fatty acid binding protein, but was not affected after preabsorption with mGOT. These results indicate that the membrane fatty acid binding protein and mGOT are structurally and functionally not related. The data also support the significance of this membrane protein in the plasma membrane binding process of long chain fatty acids.
journal_name
Mol Cell Biochemjournal_title
Molecular and cellular biochemistryauthors
Stremmel W,Diede HE,Rodilla-Sala E,Vyska K,Schrader M,Fitscher B,Passarella Sdoi
10.1007/BF00231384subject
Has Abstractpub_date
1990-10-15 00:00:00pages
191-9issue
1-2eissn
0300-8177issn
1573-4919journal_volume
98pub_type
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