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Journal of Bacteriology|July 1, 1985
Serine hydroxymethyltransferase from Escherichia coli: purification and propertiesV Schirch, S Hopkins, E Villar, et al.
Comparative Biochemistry and Physiology. B, Comparative Biochemistry|January 1, 1983
Primary structure of aspartate aminotransferase from horse heart and comparison with that of other homotopic and heterotopic isoenzymesF Martini, S Angelaccio, D Barra, et al.
Biochimica Et Biophysica Acta|August 28, 1984
Partial amino-acid sequence and cysteine reactivities of cytosolic aspartate aminotransferase from horse heartF Martini, S Angelaccio, D Barra, et al.
Protein Expression and Purification|May 1, 1996
Site-directed mutagenesis techniques in the study of Escherichia coli serine hydroxymethyltransferaseS Iurescia, I Condò, S Angelaccio, et al.
European Journal of Biochemistry|October 1, 1994
The function of arginine 363 as the substrate carboxyl-binding site in Escherichia coli serine hydroxymethyltransferaseS Delle Fratte, S Iurescia, S Angelaccio, et al.
Biotechnology and Applied Biochemistry|February 1, 1991
Assessment of sequence features in internal regions of proteinsD Barra, B Maras, M E Schininà, et al.
The Journal of Biological Chemistry|February 8, 2000
The contribution of a conformationally mobile, active site loop to the reaction catalyzed by glutamate semialdehyde aminomutaseR Contestabile, S Angelaccio, R Maytum, et al.
Biochemistry|January 14, 1992
Serine hydroxymethyltransferase: origin of substrate specificityS Angelaccio, S Pascarella, E Fattori, et al.
The Journal of Biological Chemistry|April 25, 1987
The primary structure of rabbit liver cytosolic serine hydroxymethyltransferaseF Martini, S Angelaccio, S Pascarella, et al.
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