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SERINE PROTEINASE LIKE ACTIVITY IN APOLIPOPHORIN III FROM THE HEMOLYMPH OF DESERT LOCUST, Schistocerca gregaria.
MedLine Citation:
PMID:  22499434     Owner:  NLM     Status:  Publisher    
Abstract/OtherAbstract:
Apolipophorin III (apoLp-III) has been known as a lipid transport protein of insects. Recent studies indicated the involvement of apoLp-III in immune reactions and in the control of cell destruction, but no enzymatic activity has so far been detected. In the present study, a protease from the hemolymph of Schistocerca gregaria was purified to homogeneity and its enzymatic activity was examined. Identity as chymotrypsin-like proteinase was established by its high affinity toward bulky aromatic substrates and its catalytic specificity for amide or ester bonds on the synthetic substrates, Suc-Ala-Ala-Pro-Xaa-AMC (where Xaa was Phe, Tyr, Trp, and Lys, and AMC is 7-amino-4-methyl-coumarin) and thiolbenzyl ester substrate Suc-Ala-Ala-Pro-Phe-SBzl. The sensitivity for serine protease and chymotrypsin-specific covalent inhibitors, PMSF, TPCK, and noncovalent inhibitors SGCI, showed that it is a chymotrypsin-like proteinase. It showed its maximum activity at pH 8.0 and 55°C for the hydrolysis of Suc-Ala-Ala-Pro-Tyr-AMC. According to similarities in the amino terminal sequence, molar mass (19 kDa) and retention on reversed-phase analytical high-performance liquid chromatography (HPLC) column, this protein is S. gregaria homologue of Locusta migratoria apoLp-III. Our data suggest that apoLp-III also has an inherent proteolytic activity. Results indicated that S. gregaria apoLp-III is a good catalyst and could be used as a biotechnological tool in food processing and in agricultural biotechnology.
Authors:
Zulfiqar A Malik; Sumaira Amir; István Venekei
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Publication Detail:
Type:  JOURNAL ARTICLE     Date:  2012-4-12
Journal Detail:
Title:  Archives of insect biochemistry and physiology     Volume:  -     ISSN:  1520-6327     ISO Abbreviation:  -     Publication Date:  2012 Apr 
Date Detail:
Created Date:  2012-4-13     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  8501752     Medline TA:  Arch Insect Biochem Physiol     Country:  -    
Other Details:
Languages:  ENG     Pagination:  -     Citation Subset:  -    
Copyright Information:
© 2012 Wiley Periodicals, Inc.
Affiliation:
Department of Medical Pharmacology, University of California, Davis, Iowa. zamalik@ucdavis.edu, malik52246@yahoo.com.
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