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Chemical Component and Proteomic Study of the Amphibalanus (= Balanus) amphitrite Shell.

Zhang G, He LS, Wong YH, Xu Y, Zhang Y, Qian PY - PLoS ONE (2015)

Bottom Line: The results revealed 52 proteins in the A.Amphitrite shell.

View Article: PubMed Central - PubMed

Affiliation: Environmental Science Programs and Division of Life Science, School of Science, The Hong Kong University of Science and Technology, Clearwater Bay, Kowloon, Hong Kong SAR, R. P. China.

ABSTRACT
As typical biofoulers, barnacles possess hard shells and cause serious biofouling problems. In this study, we analyzed the protein component of the barnacle Amphibalanus (= Balanus) amphitrite shell using gel-based proteomics. The results revealed 52 proteins in the A. Amphitrite shell. Among them, 40 proteins were categorized into 11 functional groups based on KOG database, and the remaining 12 proteins were unknown. Besides the known proteins in barnacle shell (SIPC, carbonic anhydrase and acidic acid matrix protein), we also identified chorion peroxidase, C-type lectin-like domains, serine proteases and proteinase inhibitor proteins in the A. Amphitrite shell. The sequences of these proteins were characterized and their potential functions were discussed. Histology and DAPI staining revealed living cells in the shell, which might secrete the shell proteins identified in this study.

No MeSH data available.


PAGE image showing protein extracts of the Amphibalanus amphitrite shell.The gel was stained by SYPRO Ruby dye (Invitrogen) and the later coomassie blue staining confirmed the molecular weight of each band in the marker. Lane I: acetic acid fraction; Lane II: 1% SDS fraction; Lane III: 10% SDS fraction. Marker from top to bottom: 170, 130, 93, 70, 53, 41, 30, 22, 14 and 9 kDa.
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pone.0133866.g001: PAGE image showing protein extracts of the Amphibalanus amphitrite shell.The gel was stained by SYPRO Ruby dye (Invitrogen) and the later coomassie blue staining confirmed the molecular weight of each band in the marker. Lane I: acetic acid fraction; Lane II: 1% SDS fraction; Lane III: 10% SDS fraction. Marker from top to bottom: 170, 130, 93, 70, 53, 41, 30, 22, 14 and 9 kDa.

Mentions: The total protein from whole barnacle shell was extracted in acetic acid, 1% SDS buffer, and 10% SDS buffer sequentially. Three fractions were collected and analyzed independently. The PAGE gel revealed clear bands for the extracts from the barnacle shell (Fig 1). The combination of MS results from all three fractions led to the identification of a total of 52 proteins in our transcriptome database (S2 Fig). Among these proteins, 20, 3, and 12 were uniquely present in the acetic acid, 1% SDS, and 10% SDS fractions, respectively. Six proteins were shared by all three fractions. Based on the KOG database, 40 proteins were categorized into 11 functional groups; the remaining 12 proteins were considered as hypothetical proteins (S1 Table).


Chemical Component and Proteomic Study of the Amphibalanus (= Balanus) amphitrite Shell.

Zhang G, He LS, Wong YH, Xu Y, Zhang Y, Qian PY - PLoS ONE (2015)

PAGE image showing protein extracts of the Amphibalanus amphitrite shell.The gel was stained by SYPRO Ruby dye (Invitrogen) and the later coomassie blue staining confirmed the molecular weight of each band in the marker. Lane I: acetic acid fraction; Lane II: 1% SDS fraction; Lane III: 10% SDS fraction. Marker from top to bottom: 170, 130, 93, 70, 53, 41, 30, 22, 14 and 9 kDa.
© Copyright Policy
Related In: Results  -  Collection

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Show All Figures
getmorefigures.php?uid=PMC4519255&req=5

pone.0133866.g001: PAGE image showing protein extracts of the Amphibalanus amphitrite shell.The gel was stained by SYPRO Ruby dye (Invitrogen) and the later coomassie blue staining confirmed the molecular weight of each band in the marker. Lane I: acetic acid fraction; Lane II: 1% SDS fraction; Lane III: 10% SDS fraction. Marker from top to bottom: 170, 130, 93, 70, 53, 41, 30, 22, 14 and 9 kDa.
Mentions: The total protein from whole barnacle shell was extracted in acetic acid, 1% SDS buffer, and 10% SDS buffer sequentially. Three fractions were collected and analyzed independently. The PAGE gel revealed clear bands for the extracts from the barnacle shell (Fig 1). The combination of MS results from all three fractions led to the identification of a total of 52 proteins in our transcriptome database (S2 Fig). Among these proteins, 20, 3, and 12 were uniquely present in the acetic acid, 1% SDS, and 10% SDS fractions, respectively. Six proteins were shared by all three fractions. Based on the KOG database, 40 proteins were categorized into 11 functional groups; the remaining 12 proteins were considered as hypothetical proteins (S1 Table).

Bottom Line: The results revealed 52 proteins in the A.Amphitrite shell.

View Article: PubMed Central - PubMed

Affiliation: Environmental Science Programs and Division of Life Science, School of Science, The Hong Kong University of Science and Technology, Clearwater Bay, Kowloon, Hong Kong SAR, R. P. China.

ABSTRACT
As typical biofoulers, barnacles possess hard shells and cause serious biofouling problems. In this study, we analyzed the protein component of the barnacle Amphibalanus (= Balanus) amphitrite shell using gel-based proteomics. The results revealed 52 proteins in the A. Amphitrite shell. Among them, 40 proteins were categorized into 11 functional groups based on KOG database, and the remaining 12 proteins were unknown. Besides the known proteins in barnacle shell (SIPC, carbonic anhydrase and acidic acid matrix protein), we also identified chorion peroxidase, C-type lectin-like domains, serine proteases and proteinase inhibitor proteins in the A. Amphitrite shell. The sequences of these proteins were characterized and their potential functions were discussed. Histology and DAPI staining revealed living cells in the shell, which might secrete the shell proteins identified in this study.

No MeSH data available.