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pro vyhledávání: '"Hyejeong Park"'
Publikováno v:
FEBS Letters. 323:271-275
Lysosomal glycosylasparaginase is encoded as a 36.5 kDa polypeptide that is post-translationally processed to subunits of 19.5 kDa (heavy) and 15 kDa (light). Recombinant glycosylasparaginase has been expressed in Spodoptera frugiperda insect cells e
Autor:
Michael P. King, Hyejeong Park, Cláudia Ferreira da Rosa Sobreira, Mercy M. Davidson, Armand F. Miranda, Yasutoshi Koga
Publikováno v:
Biochemical and biophysical research communications. 266(1)
Short-term analysis of myogenesis in respiration-deficient myoblasts demonstrated that respiratory chain dysfunction impairs muscle differentiation. To investigate long-term consequences of a deficiency in oxidative phosphorylation on myogenesis, we
Publikováno v:
Archives of biochemistry and biophysics. 328(1)
Glycosylasparaginase (EC 3.5.1.26) is a lysosomal amidase which hydrolyzes the bond between asparagine and the sugar moiety in N-linked glycoproteins. Deficiency of the enzyme results in aspartylglycosaminuria (AGU), the most common disorder of glyco
Publikováno v:
FEBS letters. 288(1-2)
The gene structure of the human lysosomal enzyme glycosylasparaginase was determined. The gene spans 13 kb and consists of 9 exons. Both 5' and 3' untranslated regions of the gene are uninterrupted by introns. A number of transcriptional elements wer