Studies on glycosyltransferases in fusion-defective conA-resistant L6 rat myoblast cell lines

The International Journal of Biochemistry
M A SpearmanE Gospodarek

Abstract

1. Sialyl- and galactosyl-transferase activities were determined in wild type and conA-resistant L6 rat myoblasts with substrates derived from fetuin, alpha 1-acid glycoprotein and bovine submaxillary mucin; fetuin was the best acceptor for both enzyme activities, whereas the mucin did not act as an acceptor. 2. The optimum pH for sialyltransferase was 6.6 in both cell lines. 3. The optimum pH for galactosyltransferase in the wild type cell line was 6.2 which was slightly higher than the value of 5.8 found for the conA-resistant cells. 4. Values for Km for both enzyme activities increased five to ten-fold in the variant cell line with both acceptors. 5. The main sialyltransferase activity was the Gal beta 1----4GlcNAc alpha 2----3sialyltransferase for N-linked chains. The galactosyltransferase was most likely the enzyme that is responsible for the synthesis of the Gal beta 1----4GlcNAc structure.

References

Feb 1, 1987·Biochemical Medicine and Metabolic Biology·R JanzenE Gospodarek
Aug 1, 1987·Biochemical Society Transactions·J C PaulsonP H Lai
Jan 1, 1986·Comparative Biochemistry and Physiology. B, Comparative Biochemistry·G Lammers, J C Jamieson
Jan 1, 1983·The International Journal of Biochemistry·M HellmanC Parfett

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Citations

May 1, 1994·Enzyme and Microbial Technology·N Jenkins, E M Curling
May 1, 1993·Comparative Biochemistry and Physiology. B, Comparative Biochemistry·J C JamiesonP G Harder
Jun 2, 2001·Comptes rendus de l'Académie des sciences. Série III, Sciences de la vie·T BourlardC Morvan
Feb 24, 2015·Skeletal Muscle·Neha Singhal, Paul T Martin

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