Cleavage by protease from Staphylococcus aureus V8: an improvement in the sequence analysis of human hemoglobin variants.
Protease from Staphylococcus aureus V8 cleaves either at glutamic residues or at both aspartic and glutamic residues, depending on the experimental conditions. In structural analyses of human hemoglobin variants, the specificity of this enzyme is of considerable interest to localize substitutions occurring in medium or large size peptides as it cleaves in smaller fragments which may be unambiguously characterized. It may also recognize the replacement of an acidic residue by the corresponding amide, or vice versa, avoiding protein sequence analysis. The various aspects of the use of protease V8 are illustrated by the study of four alpha chain hemoglobin variants concerning peptides alpha T-9 and alpha T-12b.
Vasseur
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C
INSERM U299, Hôpital de Bicêtre, Le Kremlin Bicêtre, France.
Galacteros
F
F
Groff
P
P
Wajcman
H
H
D000595:Amino Acid Sequence; D002851:Chromatography, High Pressure Liquid; D005260:Female; D014644:Genetic Variation; D006455:Hemoglobins, Abnormal / Q000235:genetics*; D006801:Humans; D006868:Hydrolysis; D008969:Molecular Sequence Data; D010449:Peptide Mapping; D012697:Serine Endopeptidases / Q000378:metabolism*; D013211:Staphylococcus aureus / Q000201:enzymology*; D013379:Substrate Specificity
D006455:Hemoglobins, Abnormal; D012697:Serine Endopeptidases; C028344:glutamyl endopeptidase