Highly reactive cysteine residues are part of the substrate binding site of mammalian dipeptidyl peptidases III

International Journal of Biochemistry and Cell Biology

Volumn 36, Issue 3, 2004, Pages 434-446

  Abramić, Marija ^a   Šimaga, Šumski ^a   Osmak, Maja ^a   Čičin Šain, Lipa ^a   Vukelić, Bojana ^a   Vlahoviček, Kristian ^b,c   Dolovčak, Ljerka ^a  

^a RUDER BO KOVI INSTITUTE   (Croatia)

^b INTERNATIONAL CENTRE FOR GENETIC ENGINEERING AND BIOTECHNOLOGY   (Italy)

^c UNIVERSITY OF ZAGREB   (Croatia)

Author keywords

Dipeptidyl peptidase III; Oxidant; Rat tissues; Reactive SH groups; Redox regulation

Indexed keywords

CYSTEINE; DIPEPTIDYL PEPTIDASE; DIPEPTIDYL PEPTIDASE III; GLUTATHIONE; HYDROGEN PEROXIDE; HYDROXYMERCURIBENZOIC ACID; PEPTIDE; THIOL DERIVATIVE; THIOL REAGENT; UNCLASSIFIED DRUG;

ANIMAL CELL; ANIMAL TISSUE; ARTICLE; BINDING SITE; CONCENTRATION RESPONSE; CONTROLLED STUDY; CYTOSOL; ENZYME ACTIVITY; ENZYME ASSAY; ENZYME BINDING; FEMALE; FLUOROMETRY; HUMAN; KINETICS; MEASUREMENT; MOLECULAR BIOLOGY; NONHUMAN; OXYGENATION; PHYSIOLOGY; RAT; WESTERN BLOTTING;

EUKARYOTA; MAMMALIA;

EID: 0347480209     PISSN: 13572725     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1357-2725(03)00267-X     Document Type: Article

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