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|dc.contributor.author||Chih Cheng Huang||en_US|
|dc.contributor.author||Yen Ling Song||en_US|
|dc.contributor.other||National Taiwan University||en_US|
|dc.contributor.other||Evolutionary Biology Centre||en_US|
|dc.identifier.citation||Developmental and Comparative Immunology. Vol.28, No.4 (2004), 279-294||en_US|
|dc.description.abstract||Transglutaminases (TG) are important for blood coagulation and post-translation remodeling of proteins. Using a plaque screening assay, we isolated cDNA encoding a novel TG from a shrimp (Penaeus monodon) hemocyte cDNA library. The TG cDNA consists of 2988 bp with an open reading frame of 2271 bp. The deduced protein has 757 amino acid residues, a calculated molecular mass of 84,713Da and an isoelectric point of 5.56. Neither a typical hydrophobic leader sequence nor a transmembrane domain could be identified from the deduced sequence. Thus, shrimp TG may be a typical cytoplasmic protein. The sequence of shrimp TG was similar to crayfish, other invertebrate and vertebrate TG sequences. Enzyme activity was detected in all organs tested. This is consistent with the widespread, low-level expression of TG mRNA. However, high levels of TG expression were detected in hematopoietic tissue. TG signals were stronger in mitotic cells, indicating that cell proliferation and TG synthesis are associated. Preliminary data showed that recombinant TG existed the enzyme activity but lacked coagulation activity. © 2003 Elsevier Ltd. All rights reserved.||en_US|
|dc.subject||Biochemistry, Genetics and Molecular Biology||en_US|
|dc.subject||Immunology and Microbiology||en_US|
|dc.title||Molecular cloning and characterization of tiger shrimp (Penaeus monodon) transglutaminase||en_US|
|Appears in Collections:||Scopus 2001-2005|
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