Isolation and characterization of T4 bacteriophage gp17 terminase, a large subunit multimer with enhanced ATPase activity

Journal of Biological Chemistry

Volumn 278, Issue 7, 2003, Pages 4618-4627

  Baumann, Richard G ^b   Black, Lindsay W ^a  

^a UNIVERSITY OF MARYLAND SCHOOL OF MEDICINE   (United States)

^b NONE

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINETRIPHOSPHATE; BACTERIA; CATALYST ACTIVITY; CHITIN; DNA; PRECIPITATION (CHEMICAL);

BACTERIOPHAGES;

ENZYMES;

ADENOSINE TRIPHOSPHATASE; ADENOSINE TRIPHOSPHATE; BACTERIAL ENZYME; DNA; GLYCEROL; GLYCOPROTEIN GP 17 TERMINASE; MONOMER; UNCLASSIFIED DRUG; DEOXYRIBONUCLEASE; PROTEIN SUBUNIT; TERMINASE, PHAGE T4; VIRUS PROTEIN;

ARTICLE; BACTERIOPHAGE T4; DNA PACKAGING; ENZYME ACTIVITY; ENZYME BINDING; ENZYME ISOLATION; ENZYME SUBUNIT; GENE; GENE 17; IMMUNOPRECIPITATION; MOLECULAR CLONING; NONHUMAN; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRIORITY JOURNAL; PROTEIN DENATURATION; PROTEIN PURIFICATION; PROTEIN SECRETION; ENZYMOLOGY; ISOLATION AND PURIFICATION; METABOLISM; PHYSIOLOGY; PROTEIN CONFORMATION; VIRUS ASSEMBLY;

BACTERIA (MICROORGANISMS); UNIDENTIFIED BACTERIOPHAGE;

ADENOSINE TRIPHOSPHATASES; BACTERIOPHAGE T4; ENDODEOXYRIBONUCLEASES; PROTEIN CONFORMATION; PROTEIN SUBUNITS; VIRAL PROTEINS; VIRUS ASSEMBLY;

EID: 0038751848     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M208574200     Document Type: Article

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