"6464","13","archive","30",,,"disk0/00/00/64/64","2013-01-24 11:30:02","2017-10-17 04:13:25","2013-01-24 11:30:02","article",,,"show","Library-ICRISAT@cgiar.org",,,"","","","","","","","","","",,,,"Goudru","H G","","","","","","","Sharma","H C","","","","",,,,,"","",,,,,"","","Gulbarga University(Gulbarga)","","Purification and characterization of prophenoloxidase from cotton bollworm, Helicoverpa armigera","pub","s2.7","","","restricted",,,"copper binding B site;
Helicoverpa armigera;
Kojic acid;
prophenoloxidase
",,"We are thankful to University Grant Commission (UGC)
for providing the fellowship under UGC-RFSMS scheme
during this work. This research was supported by a research
grant from the Department of Science and Technology
(DST), New Delhi, to K. Sreeramulu and University Grant
Commission under Special Assistance Program (UGCSAP),
New Delhi, India. We also thank the Director Rabindra
R. J and Dr. Jalali, S. K., Principal Scientist, NBAII,
Bangalore, India, for providing the lab facilities throughout
this work","Phenoloxidases are oxidative enzymes, which play an important role in both cell mediated and humoral immunity. Purification and biochemical characterization of prophenoloxidase from cotton bollworm, Helicoverpa armigera (Hübner) were carried out to study its biochemical properties. Prophenoloxidase consists of a single polypeptide chain with a relative molecular weight of 85 kDa as determined by SDS–PAGE, MALDI–TOF MS and LC–ESI MS. After the final step, the enzyme showed 71.7 fold of purification with a recovery of 49.2%. Purified prophenoloxidase showed high specific activity and homology with phenoloxidase subunit-1 of Bombyx mori and the conserved regions of copper binding (B) site of phenoloxidase. Purified prophenoloxidase has pH optima of 6.8 and has high catalytic efficiency towards the dopamine as a substrate in comparison to catechol and L-Dopa. The PO activity was strongly inhibited by phenylthiourea, thiourea, dithiothreitol and kojic acid.","2013","published",,"Entomological Research","43","1","John Wiley & Sons, Inc. in association with the Entomological Society of Korea",,"55-62",,,,,,,,,,,"TRUE",,"1748-5967",,,,,,"","http://dx.doi.org/10.1111/1748-5967.12002","http://scholar.google.co.in/scholar?as_q=%22Purification+and+characterization+of+prophenoloxidase+from+cotton+bollworm%2C+Helicoverpa+armigera%22&as_epq=&as_oq=&as_eq=&as_occt=title&as_sauthors=&as_publication=&as_ylo=&as_yhi=&btnG=&hl=en&as_sdt=0%2C5","pub",,"Government of India - Department of Science and Technology","University Grant Commission under Special Assistance Program(UGC-SAP)",,,,,,"",,,,,,,"",,,,,"",,,,,"","",,,,,"","",,,,,
"6464",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,"Kumar","Sathish","","",,,,,,,,,,,,,,,,,,,,,,,"Indian Institute of Science(Bangalore)",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,"Government of India- University Grant Commission",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,
"6464",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,"Jayalakshmi","S K","","",,,,,,,,,,,,,,,,,,,,,,,"University of Agricultural Sciences(Bangalore)",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,
"6464",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,"Ballal","C R","","",,,,,,,,,,,,,,,,,,,,,,,"National Bureau of Agriculturally Important Insects(Bangalore)",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,
"6464",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,"Sharma","H C","","",,,,,,,,,,,,,,,,,,,,,,,"ICRISAT(Patancheru)",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,
"6464",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,"Sreeramulu","K","","",,,,,,,,,,,,,,,,,,,,,,,"India",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,