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Journal of Biological Chemistry

Volumn 271, Issue 39, 1996, Pages 24236-24241

Cysteine mutations in the MAM domain result in monomeric meprin and alter stability and activity of the proteinase

(3) Marchand, Petra a Volkmann, Marika b Bond, Judith S a

a PENN STATE COLLEGE OF MEDICINE (United States)

b DUPONT COMPANY (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CYSTEINE; DISULFIDE; MEPRIN; PROTEINASE;

AMINO ACID SUBSTITUTION; ARTICLE; CELL SURFACE; DIMERIZATION; ENZYME ACTIVITY; ENZYME INACTIVATION; ENZYME STABILITY; GLYCOSYLATION; HUMAN; HUMAN CELL; INTRACELLULAR TRANSPORT; OLIGOMERIZATION; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN PROTEIN INTERACTION; STRUCTURE ACTIVITY RELATION;

ANIMALS; CASEINS; CELL LINE; DISULFIDES; ENDOPEPTIDASES; GLYCOPROTEINS; GLYCOSYLATION; HEAT; HUMANS; MACROMOLECULAR SUBSTANCES; MERCAPTOETHANOL; METALLOENDOPEPTIDASES; MICE; OXIDATION-REDUCTION; PROTEIN DENATURATION; PROTEIN PROCESSING, POST-TRANSLATIONAL; STRUCTURE-ACTIVITY RELATIONSHIP;

EID: 0029793539 PISSN: 00219258 EISSN: None Source Type: Journal
DOI: 10.1074/jbc.271.39.24236 Document Type: Article

Times cited : (41)

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