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Biochemistry

Title:		Purification and biochemical characterization of recombinant hirudin produced by Saccharomyces cerevisiae
Author(s):		Riehl-Bellon N; Carvallo D; Acker M; Van Dorsselaer A; Marquet M; Loison G; Lemoine Y; Brown SW; Courtney M; Roitsch C;
Address:		"Transgene S.A., Strasbourg, France"
Journal Title:		Biochemistry
Year:		1989
Volume:		28
Issue:		7
Page Number:		2941 - 2949
DOI:		10.1021/bi00433a030
ISSN/ISBN:		0006-2960 (Print) 0006-2960 (Linking)
Abstract:		"Recombinant hirudin was produced by the yeast Saccharomyces cerevisiae using the alpha-pheromone prepro sequence to direct its secretion into the culture medium. The secreted hirudin was isolated to greater than or equal to 95% purity as measured by 205-nm absorbance integration from a reverse-phase chromatogram. One major activity peak corresponding to the complete, correctly processed molecule and two minor activity peaks corresponding to C-terminally truncated forms were identified. The primary structure of the major peak, determined by N-terminal sequencing of tryptic peptides, was that predicted from the cDNA sequence, and the molecular mass analyzed by fast atom bombardment mass spectrometry (FAB-MS) was 6892.6 (calculated 6892.5). UV spectral analysis suggested that, in contrast to the natural molecule, recombinant hirudin produced by S. cerevisiae is not sulfated"
Keywords:		"Amino Acid Sequence Chromatography, High Pressure Liquid Escherichia coli/genetics Genetic Vectors Hirudins/*isolation & purification Molecular Sequence Data Peptide Mapping Plasmids Recombinant Proteins/isolation & purification Saccharomyces cerevisiae/*;"
Notes:		"MedlineRiehl-Bellon, N Carvallo, D Acker, M Van Dorsselaer, A Marquet, M Loison, G Lemoine, Y Brown, S W Courtney, M Roitsch, C eng 1989/04/04 Biochemistry. 1989 Apr 4; 28(7):2941-9. doi: 10.1021/bi00433a030"