Abstract：
:One cDNA clone was purified from an adult Clonorchis sinensis cDNA library, and its deduced polypeptide sequence was found to be homologous with myosin regulatory light chain (MRLC) of invertebrates and vertebrates. Two amino-acid residues, Thr and Ser, were conserved at the phosphorylation sites that regulate the function of MRLCs. Recombinant C. sinensis MRLC (rCsMRLC) protein was produced and purified from Escherichia coli, and mouse anti-CsMRLC immune sera recognized a protein of molecular weight 24 kDa from a soluble protein preparation of C. sinensis. The CsMRLC protein was immunohistochemically localized to the muscle fibers of the subtegumental muscle layer and to the muscles of oral and ventral suckers. However, the rCsMRLC protein proved to be less useful antigen for the serodiagnosis of human clonorchiasis.
journal_name
Parasitol Resjournal_title
Parasitology researchauthors
Kwon YD,Cho PY,Hong SJdoi
10.1007/s00436-005-1376-9subject
Has Abstractpub_date
2005-08-01 00:00:00pages
21-6issue
1eissn
0932-0113issn
1432-1955journal_volume
97pub_type
杂志文章abstract：:Knowledge of vector species composition and monitoring their change over time is critical to evaluate malaria transmission and assess control interventions. This is especially important in countries such as Botswana, where malaria transmission is subjected to fluctuations due to climate variability. Another important ...
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