TẠO DÒNG VÀ PHÂN TÍCH TRÌNH TỰ GEN SERINE PROTEASE THỦY PHÂN FIBRIN TỪ GIUN QUẾ (Perionyx excavatus)

Author(s):  
Trần Quốc Dung ◽  
Đặng Phước Hải

Lumbrokinase của giun quế (Perionyx excavatus) là một enzyme thủy phân fibrin. Trong nghiên cứu này, cDNA mã hóa gen lumbrokinase được khuếch đại với cặp mồi đặc hiệu được thiết kế dựa vào trình tự gen mã hóa lumbrokinase trên GenBank với mã số DQ234061. Đoạn cDNA có kích thước 726 bp được tạo dòng với vector pCR®2.1. Trình tự nucleotide của cDNA được so sánh với trình tự của gen lumbrokinase của các loài giun đất Eisenia fetida (mã số DQ234061), Lumbricus bimastus (mã số AY187629) và Lumbricus rubellus (mã số U25644) trên GenBank và có độ tương đồng lần lượt là 52,02%; 50,06% và 48,03%. Từ khóa: cDNA, lumbrokinase, giun quế (Perionyx excavatus).

2020 ◽  
Vol 23 (2) ◽  
pp. 99-104
Author(s):  
Agus Mulyadi Purnawanto ◽  
Yugi R. Ahadiyat ◽  
Achmad Iqbal ◽  

AbstractThe objective of this study was to determine the capacity of Lumbricus rubellus, Eisenia fetida and Eudrilus eugeniae earthworms in vermicompost production utilizing mushroom waste substrate based on weight; number and weight loss of earthworms; temperature; pH; moisture content of media; and C/N ratio. The results showed that, by using 42 g of E. eugeniae, E. fetida and L. rubellus earthworms, there was an increase in weight of earthworms and vermicompost by more than 300% and 75%, respectively. In general, these three species of earthworms were able to produce vermicompost in compliance with quality standards, showing C/N ratio lower than 20.


2010 ◽  
Vol 2010 ◽  
pp. 1-13 ◽  
Author(s):  
Rong Pan ◽  
Zi-Jian Zhang ◽  
Rong-Qiao He

The alimentary tract of earthworm secretes a group of proteases with a relative wide substrate specificity. In 1983, six isozymes were isolated from earthworm with fibrinolytic activities and called fibriniolytic enzymes. So far, more isozymes have been found from different earthworm species such asLumbricus rubellusandEisenia fetida. For convenience, the proteases are named on the basis of the earthworm species and the protein function, for instance,Eisenia fetidaprotease (EfP). The proteases have the abilities not only to hydrolyze fibrin and other protein, but also activate proenzymes such as plasminogen and prothrombin. In the light of recent studies, eight of theEfPs contain oligosaccharides chains which are thought to support the enzyme structure. Interestingly,EfP-II has a broader substrate specificity presenting alkaline trypsin, chymotrypsin and elastase activities, butEfP-III-1 has a stricter specificity. The protein crystal structures show the characteristics in their specificities. Earthworm proteases have been applied in several areas such as clinical treatment of clotting diseases, anti-tumor study, environmental protection and nutritional production. The current clinical utilizations and some potential new applications of the earthworm protease will be discussed in this paper.


2018 ◽  
Vol 52 (1) ◽  
pp. 59-64
Author(s):  
A. A. Antipov ◽  
T. I. Bakhur ◽  
D. V. Feshchenko ◽  
T. A. Romanishina ◽  
N. V. Avramenko ◽  
...  

Abstract The article presents the data on prevalence and intensity of earthworms’ infection with metastrongylid larvae in pork production enterprises of Kyiv and Zhytomyr Regions of Ukraine. In the investigated areas, six species of lumbricids were collected and identifi ed: Eisenia fetida (Savigny, 1826), Aporrectodea rosea (Savigny, 1826), A. caliginosa (Savigny, 1826), Dendrodrilus rubidus (Savigny, 1826), Lumbricus rubellus (Linnaeus, 1758), L. terrestris (Linnaeus, 1758). Th e studies were carried out from April to September, 2016, both in pig farms and on pastures. We observed no pronounced changes in prevalence and intensity of infection during the warm period of the year. Th e highest infection rates were detected in earthworms living under the wooden floor of pigpens and in its cracks. In the studied localities, metastrongylid larvae were found in the most common worms of the Lumbricidae family: E. foetida, D. rubidus, A. caliginosa, and L. rubellus.


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