Hydrolytic enzymes conjugated to quantum dots mostly retain whole catalytic activity

Biochimica et Biophysica Acta - General Subjects

Volumn 1840, Issue 9, 2014, Pages 2935-2943

  Iyer, Aditya ^a   Chandra, Anil ^a   Swaminathan, Rajaram ^a  

^a INDIAN INSTITUTE OF TECHNOLOGY GUWAHATI   (India)

Author keywords

Acetylcholinesterase; Alkaline phosphatase; Enzyme catalytic activity; Hen egg white lysozyme; Luminescence; Semiconductor nanocrystals

Indexed keywords

ACETYLCHOLINESTERASE; ALKALINE PHOSPHATASE; AVIDIN; BIOTIN; HEN EGG WHITE LYSOZYME; HYDROLASE; LYSINE; LYSOZYME; QUANTUM DOT; STREPTAVIDIN; UNCLASSIFIED DRUG;

ARTICLE; BIOTINYLATION; CATALYSIS; CHEMISTRY; CONCENTRATION (PARAMETERS); ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME SUBSTRATE; GEL ELECTROPHORESIS; IONIC STRENGTH; LUMINESCENCE; LUMINESCENCE SPECTROMETRY; PRIORITY JOURNAL; SPECTROMETRY;

ACETYLCHOLINESTERASE; ALKALINE PHOSPHATASE; ENZYME CATALYTIC ACTIVITY; HEN EGG WHITE LYSOZYME; LUMINESCENCE; SEMICONDUCTOR NANOCRYSTALS;

ACETYLCHOLINESTERASE; ALKALINE PHOSPHATASE; ANIMALS; BIOTIN; BIOTINYLATION; CATALYSIS; CHICKENS; ENZYME STABILITY; MURAMIDASE; QUANTUM DOTS; STREPTAVIDIN;

EID: 84903712082     PISSN: 03044165     EISSN: 18728006     Source Type: Journal    
DOI: 10.1016/j.bbagen.2014.06.003     Document Type: Article

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