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Article

Cleavage by protease from Staphylococcus aureus V8: an improvement in the sequence analysis of human hemoglobin variants.

Journal of biochemical and biophysical methods - 1 Apr 1991

Vasseur C, Galacteros F, Groff P, Wajcman H

Abstract excerpt

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...

Topics

Amino Acid Sequence
Chromatography, High Pressure Liquid
Female
Genetic Variation
Hemoglobins, Abnormal
Humans
Hydrolysis
Molecular Sequence Data
Peptide Mapping
Serine Endopeptidases
Staphylococcus aureus

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Identifiers

PMID: 1865052
DOI: 10.1016/0165-022x(91)90068-8

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-1865052-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

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