Structural study of Carcinus maenas hemocyanin by native ESI-MS: Interaction with L-lactate and divalent cations

Proteins: Structure, Function and Bioinformatics

Volumn 77, Issue 3, 2009, Pages 589-601

  Bruneaux, Matthieu ^a,b   Terrier, Peran ^c,d   Leize, Emmanuelle ^c   Mary, Jean ^a,b,e   Lallier, François H ^a,b   Zal, Franck ^a,b,f  

^a SORBONNE UNIVERSITÉ   (France)

^b STATION BIOLOGIQUE DE ROSCOFF   (France)

^c Institut de Chimie   (France)

^d UNIVERSITÉ D EVRY VAL D ESSONNE   (France)

^e UNIVERSITÉ PARIS DESCARTES   (France)

^f STATION BIOLOGIQUE   (France)

Author keywords

Dissociation; Hemocyanin lactate; Macromolecule; Mass spectrometry; Noncovalent interactions; Physiological modulator; Reassociation

Indexed keywords

DIVALENT CATION; EDETIC ACID; FORMIC ACID; HEMOCYANIN; LACTIC ACID; PROTEIN SUBUNIT;

ACIDIFICATION; ALKALINITY; ARTICLE; BINDING SITE; CHELATION; CRAB; DISSOCIATION; ELECTROSPRAY MASS SPECTROMETRY; HEMOLYMPH; NONHUMAN; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN INTERACTION;

ALLOSTERIC REGULATION; ANIMALS; BINDING SITES; BRACHYURA; CATIONS; CHELATING AGENTS; EDETIC ACID; FORMIC ACIDS; HEMOCYANIN; HEMOLYMPH; LACTIC ACID; MASS SPECTROMETRY; SPECTROMETRY, MASS, ELECTROSPRAY IONIZATION;

CARCINUS MAENAS;

EID: 70349330156     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.22471     Document Type: Article

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