eprintid: 6464
rev_number: 13
eprint_status: archive
userid: 30
dir: disk0/00/00/64/64
datestamp: 2013-01-24 11:30:02
lastmod: 2017-10-17 04:13:25
status_changed: 2013-01-24 11:30:02
type: article
metadata_visibility: show
contact_email: Library-ICRISAT@cgiar.org
creators_name: Goudru, H G
creators_name: Kumar, Sathish
creators_name: Jayalakshmi, S K
creators_name: Ballal, C R
creators_name: Sharma, H C
creators_name: Sreeramulu, K
icrisatcreators_name: Sharma, H C
affiliation: Gulbarga University(Gulbarga)
affiliation: Indian Institute of Science(Bangalore)
affiliation: University of Agricultural Sciences(Bangalore)
affiliation: National Bureau of Agriculturally Important Insects(Bangalore)
affiliation: ICRISAT(Patancheru)
affiliation: India
title: Purification and characterization of prophenoloxidase from cotton bollworm, Helicoverpa armigera
ispublished: pub
subjects: s2.7
full_text_status: restricted
keywords: copper binding B site;
Helicoverpa armigera;
Kojic acid;
prophenoloxidase

note: 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
abstract: 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.
date: 2013
date_type: published
publication: Entomological Research
volume: 43
number: 1
publisher: John Wiley & Sons, Inc. in association with the Entomological Society of Korea
pagerange: 55-62
refereed: TRUE
issn: 1748-5967
official_url: http://dx.doi.org/10.1111/1748-5967.12002
related_url_url: 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
related_url_type: pub
funders: Government of India - Department of Science and Technology
funders: Government of India- University Grant Commission
projects: University Grant Commission under Special Assistance Program(UGC-SAP)
citation:   Goudru, H G and Kumar, Sathish and Jayalakshmi, S K and Ballal, C R and Sharma, H C and Sreeramulu, K  (2013) Purification and characterization of prophenoloxidase from cotton bollworm, Helicoverpa armigera.  Entomological Research, 43 (1).  pp. 55-62.  ISSN 1748-5967     
document_url: http://oar.icrisat.org/6464/1/EntomologicalRes_43_55-62_2013.pdf