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Cleavage by Protease From Staphylococcus Aureus V8: An Improvement in the Sequence Analysis of Human Hemoglobin Variants

Cleavage by Protease From Staphylococcus Aureus V8: An Improvement in the Sequence Analysis of Human Hemoglobin Variants

C Vasseur, F Galacteros, P Groff, H Wajcman

J Biochem Biophys Methods. 1991 Apr;22(3):195-205.

PMID: 1865052

Abstract:

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.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
AP66676435-A	Endoproteinase Glu-C from Staphylococcus aureus V8		66676-43-5	Price

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