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Volumn 1645, Issue 1, 2003, Pages 81-88
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Isolation by zinc-affinity chromatography of the histidine-proline-rich- glycoprotein molecule associated with rabbit skeletal muscle AMP deaminase: Evidence that the formation of a protein-protein complex between the catalytic subunit and the novel component is critical for the stability of the enzyme
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Author keywords
AMP deaminase structure; Histidine proline rich glycoprotein; Immobilized metal ion affinity chromatography
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Indexed keywords
ADENOSINE PHOSPHATE DEAMINASE;
GLYCOPEPTIDASE;
GLYCOPROTEIN;
HISTIDINE DERIVATIVE;
ISOENZYME;
MUSCLE ENZYME;
PEPTIDE DERIVATIVE;
PROLINE DERIVATIVE;
ZINC;
ADENOSINE MONOPHOSPHATE DEAMINASE;
DRUG DERIVATIVE;
HISTIDINE;
HISTIDINE RICH PROTEINS;
HISTIDINE-RICH PROTEINS;
NITRIC OXIDE;
NITROGEN OXIDE;
PROLINE;
PROLINE NITRIC OXIDE;
PROLINE-NITRIC OXIDE;
PROTEIN;
AFFINITY CHROMATOGRAPHY;
AMINO TERMINAL SEQUENCE;
ARTICLE;
CATALYSIS;
COMPLEX FORMATION;
DENATURATION;
ENZYME ACTIVITY;
GLYCOSYLATION;
MOLECULAR WEIGHT;
MOLECULE;
NONHUMAN;
PLASMA;
PRIORITY JOURNAL;
PROTEIN ISOLATION;
PROTEIN STABILITY;
RABBIT;
SKELETAL MUSCLE;
ANIMAL;
BINDING SITE;
CHEMISTRY;
ENZYME STABILITY;
ISOLATION AND PURIFICATION;
METABOLISM;
METHODOLOGY;
PH;
POLYACRYLAMIDE GEL ELECTROPHORESIS;
PROTEIN QUATERNARY STRUCTURE;
ORYCTOLAGUS CUNICULUS;
AMP DEAMINASE;
ANIMALS;
BINDING SITES;
CHROMATOGRAPHY, AFFINITY;
ELECTROPHORESIS, POLYACRYLAMIDE GEL;
ENZYME STABILITY;
GLYCOPROTEINS;
HISTIDINE;
HYDROGEN-ION CONCENTRATION;
MUSCLE, SKELETAL;
NITRIC OXIDE;
NITROGEN OXIDES;
PROLINE;
PROTEIN STRUCTURE, QUATERNARY;
PROTEINS;
RABBITS;
ZINC;
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EID: 0037474256
PISSN: 15709639
EISSN: None
Source Type: Journal
DOI: 10.1016/S1570-9639(02)00527-7 Document Type: Article |
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Times cited : (22)
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References (34)
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