Review
doi: 10.1016/j.biocel.2005.04.006.
Impairment of IGF-I gene splicing and MGF expression associated with muscle wasting
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- PMID: 16125110
- DOI: 10.1016/j.biocel.2005.04.006
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Review
Impairment of IGF-I gene splicing and MGF expression associated with muscle wasting
Int J Biochem Cell Biol.
2005 Oct.
Erratum in
- Int J Biochem Cell Biol. 2006 Mar;38(3):480
Corrected and republished in
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Impairment of IGF-I gene splicing and MGF expression associated with muscle wasting.Int J Biochem Cell Biol. 2006 Mar;38(3):481-9. doi: 10.1016/j.biocel.2005.10.001. Int J Biochem Cell Biol. 2006. PMID: 16463438 Review.
Abstract
An aminopeptidase was purified from bovine skeletal muscle by ammonium sulfate fractionation and by successive chromatographies of DEAE-cellulose, Sehacryl S-200, phenyl-sepharose CL-4B, hydroxyapatite and Hi-Trap chelating HP columns. The aminopeptidase was purified about 14-fold over the crude extract with a yield of 1.0% activity. The molecular mass of the enzyme was found to be 58 kDa on SDS-PAGE. The enzyme activity was enhanced by the addition of some anions, such as Cl(-), NO(3)(-) and SCN(-), which is the most unique property of this enzyme. While, the activity was strongly inhibited by bestatin, PMSF and puromycin, suggesting that it was a serine protease. In addition, this enzyme was identical with leukotriene (LT) A4 hydrolase, converting LTA4 to LTB4.
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