scholarly journals Expression, Affinity, and Functional Characterization of the Specific Binding of Two Putative Pheromone-Binding Proteins in the Omnivorous German Cockroach Blattella germanica

2020 ◽  
Vol 68 (47) ◽  
pp. 13573-13583
Author(s):  
Hong Wang ◽  
Yun-Feng Ma ◽  
Mei-Mei Wang ◽  
Guang-Lei Chen ◽  
Youssef Dewer ◽  
...  
Keyword(s):  
Binding Proteins ◽  
Specific Binding ◽  
Functional Characterization ◽  
Blattella Germanica ◽  
German Cockroach ◽  
Pheromone Binding Proteins ◽  
Cockroach Blattella Germanica

Proteome mining for novel IgE-binding proteins from the German cockroach (Blattella germanica) and allergen profiling of patients

2011 ◽  
Vol 5 (3-4) ◽  
pp. 202-202
Author(s):  
Jiing-Guang Chuang ◽  
Song-Nan Su ◽  
Bor-Luen Chiang ◽  
How-Jing Lee ◽  
Lu-Ping Chow
Keyword(s):  
Binding Proteins ◽  
Blattella Germanica ◽  
German Cockroach ◽  
Ige Binding ◽  
Cockroach Blattella Germanica

scholarly journals Identification and functional characterization of an ovarian aquaporin from the cockroach Blattella germanica L. (Dictyoptera, Blattellidae)

2011 ◽  
Vol 214 (22) ◽  
pp. 3895-3895 ◽  
Author(s):  
A. Herraiz ◽  
F. Chauvigne ◽  
J. Cerda ◽  
X. Belles ◽  
M.-D. Piulachs
Keyword(s):  
Functional Characterization ◽  
Blattella Germanica ◽  
Cockroach Blattella Germanica

scholarly journals Purification and Partial Characterization of Agglutinin Lectin from Heamolymph of German Cockroach, Blattella germanica

2020 ◽  
Author(s):  
Zohreh Nabavi ◽  
Mozhgan Baniardalani ◽  
Hamidreza Basseri
Keyword(s):  
Molecular Weight ◽  
Specific Binding ◽  
German Cockroach ◽  
Exchange Chromatography ◽  
Inhibition Assay ◽  
Human Red Blood Cells ◽  
Sds Page ◽  
Cockroach Blattella Germanica ◽  
Binding Lectin

Background: Lectin molecules have crucial biological role in insects’ immune system. The aim of present study was to find the agglutinin activities in haemolymph of German cockroach, Belatella germanica with appropriate screening and purification. Methods: The heamolymph of cockroach was collected and agglutinin test performed against different animal and human red blood cells (RBC). Then sugar inhibition assay was carried out to find carbohydrate specific binding lectin. The proteins of haemolymph was purified using ion-exchange chromatography (HPLC) and each fraction was tested for agglutinin activity. Finally the molecular weight of the agglutinin protein was determined using SDS-page. Results: The most agglutinin activity of haemolymph was found against RBC of mouse at titer 1/128ml/L dilution and sugar inhibition assay showed that fucos, N-acetyglucoseamine and galactose reduced titer of agglutinin to ½ml/L. Only one fraction of heamolymph at rotation time of 36 minute showed agglutinin activity. The molecular weight of this lectin was measured as 120Kds. Conclusion: The range of agglutinin activities against different RBC indicates that the isolated lectin is not specific for a particular carbohydrate. In addition, the isolated lectin at low concentration present in heamolymph should be an innate lactin not secreted, because we found it without any trigger immunity of the insect.

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