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Biochimica Et Biophysica Acta|July 24, 1998
Kinetic properties and thermal stabilities of mutant forms of mitochondrial aspartate aminotransferaseA Azzariti, R A Vacca, S Giannattasio, et al.Biochimica Et Biophysica Acta|November 8, 1985
The primary structure of mitochondrial aspartate aminotransferase from human heartF Martini, S Angelaccio, D Barra, et al.Biochemistry and Molecular Biology International|November 1, 1995
Changes in enzyme levels in hypertensive heart tissueA Atlante, F Abruzzese, T M Seccia, et al.The Journal of Biological Chemistry|December 5, 1988
Mutants of translational components that alter reading frame by two steps forward or one step backM B Falahee, R B Weiss, M O'Connor, et al.The Journal of Clinical Investigation|June 1, 1994
Mutation of the fumarase gene in two siblings with progressive encephalopathy and fumarase deficiencyT Bourgeron, D Chretien, J Poggi-Bach, et al.The Biochemical Journal|November 1, 1972
The primary structure of aspartate aminotransferase from pig heart muscle. Partial sequences determined by digestion with pepsin and trypsi trypsinS Doonan, H J Doonan, F Riva, et al.The Biochemical Journal|August 1, 1973
The primary structure of aspartate aminotransferase from pig heart muscle. Partial sequences determined by digestion with thermolysin and elastaseF Bossa, D Barra, M Carloni, et al.European Journal of Biochemistry|December 11, 1976
An assessment of some of the methods available for the determination of molecular weights of proteins as applied to aspartate aminotransferase from pig heartB E Banks, S Doonan, M Flogel, et al.The Biochemical Journal|September 1, 1975
The primary structure of aspartate aminotransferase from pig heart muscle. Digestion with a proteinase having specificity for lysine residuesS Doonan, H J Doonan, R Hanford, et al.Pageof 5