| View Larger Image | Identification of a type of human IgG-like protein in shrimp Penaeus vannamei by mass spectrometry [An article from: Journal of Experimental Marine Biology and Ecology] | Digitalby Y. Zhang (Author), S. Wang (Author), X. Peng (Author)
| List Price: | $8.95 | | | Available: | Available for download now |
| | Binding: | Digital | | Publisher: | Elsevier | | Publication Date: | April 07, 2004 |
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Product Description
This digital document is a journal article from Journal of Experimental Marine Biology and Ecology, published by Elsevier in 2004. The article is delivered in HTML format and is available in your Amazon.com Media Library immediately after purchase. You can view it with any web browser.Description: Recently, infectious diseases have delayed the growth of shrimp aquaculture. Interest has been focused on immune molecules and defense mechanisms to reduce these diseases in shrimp aquaculture. In invertebrates, various immunoglobulin superfamily (IgSF) molecules have been characterized in body tissues and fluids, which play a significant role in innate defense. In the current study, we found that a protein in shrimp serum, referred as an IgG-like protein, could be reacted with goat anti-human IgG, specifically. The IgG-like protein was purified from the serum of shrimp Penaeus vannamei by affinity chromatography using CNBr-activated sepharose 4B. The purified protein was subsequently analysed using one-dimensional sodium sulphate-polyacrylamide gel electrophoresis (1-DE), two-dimensional sodium sulphate-polyacrylamide gel electrophoresis (2-DE) and immunoblotting. Furthermore, matrix-assisted laser desorption ionization time-of-flight (MALDI-TOF) mass spectrometry and quadrupole time-of-flight (Q-TOF) tandem mass spectrometry methods were used for peptide mass fingerprint (PMF) and sequencing of the protein, respectively. Sequence information and PMF queried against the NCBI database confirmed the identity of the protein as hemocyanin. Conserved domain search showed that there was an Ig-like conserved domain of 252 amino acid residues in the C-terminus of arthropoda hemocyanins. In addition, four and one conserved regions were found between hemocyanin and human Ig heavy chain and Ig kappa chain, respectively. These results indicate that in addition to copper-binding domains hemocyanin has an Ig-like conserved domain, which would confer some new functions to multifunctional respiratory pigment of crustaceans. |
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