Co-immobilization of PEGylated Aspergillus flavipes l-methioninase with glutamate dehydrogenase: A novel catalytically stable anticancer consortium

Enzyme and Microbial Technology

Volumn 54, Issue 1, 2014, Pages 59-69

  El Sayed, Ashraf S A ^a   Ibrahim, Hend ^a   Sitohy, Mahmoud Z ^b  

^a ZAGAZIG UNIVERSITY   (Egypt)

^b Zagazig University   (Egypt)

Author keywords

AfMETase; AfMETase GDH; PEG AfMETase; PEG AfMETase GDH

Indexed keywords

AFMETASE; AFMETASE-GDH; ASPERGILLUS FLAVIPES; GLUTAMATE DEHYDROGENASE; PEG-AFMETASE; PEG-AFMETASE-GDH; PHARMACOKINETIC PROPERTIES; THERAPEUTIC EFFICIENCY;

ASPERGILLUS; ENZYMES; PROTEOLYSIS;

AMINO ACIDS;

CYSTEINE; FUNGAL ENZYME; GLUTAMATE DEHYDROGENASE; GLUTARALDEHYDE; HOMOCYSTEINE; HYDROXYLAMINE; METHIONINE; METHIONINE GAMMA LYASE; PROPARGYLGLYCINE; PROSTAGLANDIN E;

ANTIGENICITY; ARTICLE; ASPERGILLUS FLAVIPES; BINDING AFFINITY; CHEMICAL PROCEDURES; CONJUGATION; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME DEGRADATION; ENZYME IMMOBILIZATION; ENZYME STABILITY; ENZYME STRUCTURE; ENZYME SUBSTRATE COMPLEX; HYPERAMMONEMIA; IN VIVO STUDY; NONHUMAN; PEGYLATION; POLYACRYLAMIDE GEL ELECTROPHORESIS; SURFACE PROPERTY;

ASPERGILLUS FLAVIPES;

AFMETASE; AFMETASE-GDH; PEG-AFMETASE; PEG-AFMETASE-GDH;

ANTINEOPLASTIC AGENTS; ASPERGILLUS; CARBON-SULFUR LYASES; CATALYTIC DOMAIN; ENZYME STABILITY; ENZYMES, IMMOBILIZED; FUNGAL PROTEINS; GLUTAMATE DEHYDROGENASE; HOT TEMPERATURE; HYDROGEN-ION CONCENTRATION; KINETICS; POLYETHYLENE GLYCOLS;

EID: 84888026247     PISSN: 01410229     EISSN: 18790909     Source Type: Journal    
DOI: 10.1016/j.enzmictec.2013.10.004     Document Type: Article

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