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Fish Physiology and Biochemistry

, Volume 41, Issue 3, pp 789–802 | Cite as

Proteomic profiling of white muscle from freshwater catfish Rita rita

  • Bimal Prasanna Mohanty
  • Tandrima Mitra
  • Sudeshna Banerjee
  • Soma Bhattacharjee
  • Arabinda Mahanty
  • Satabdi Ganguly
  • Gopal Krishna Purohit
  • Dhanasekar Karunakaran
  • Sasmita Mohanty
Article

Abstract

Muscle tissues contribute 34–48 % of the total body mass in fish. Proteomic analysis enables better understanding of the skeletal muscle physiology and metabolism. A proteome map reflects the general fingerprinting of the fish species and has the potential to identify novel proteins which could serve as biomarkers for many aspects of aquaculture including fish physiology and growth, flesh quality, food safety and aquatic environmental monitoring. The freshwater catfish Rita rita of the family Bagridae inhabiting the tropical rivers and estuaries is an important food fish with high nutritive value and is also considered a species of choice in riverine pollution monitoring. Omics information that could enhance utility of this species in molecular research is meager. Therefore, in the present study, proteomic analysis of Rita rita muscle has been carried out and functional genomics data have been generated. A reference muscle proteome has been developed, and 23 protein spots, representing 18 proteins, have been identified by MALDI-TOF/TOF-MS and LC-MS/MS. Besides, transcript information on a battery of heat shock proteins (Hsps) has been generated. The functional genomics information generated could act as the baseline data for further molecular research on this species.

Keywords

Muscle proteomics Rita rita Biomarkers Flesh quality Aquatic pollution biomonitoring 

Notes

Acknowledgments

This work was supported by the Indian Council of Agricultural Research, New Delhi, under CIFRI Core Project No. FHE/ER/07/06/005 to BPM. The authors are thankful to the Director, CIFRI, Barrackpore, for the facilities and encouragement. The authors wish to record their sincere appreciation to the unknown reviewers for meticulously reading the manuscript and offering suggestions that helped in substantially improving it.

Conflict of interest

The authors declare that they have no conflict of interests.

Supplementary material

10695_2015_46_MOESM1_ESM.pdf (1.3 mb)
ESM_1 The homology of mapped peptides with other species used for identification, the amino acid sequences of identified peptides and MALDI-TOF/TOF mass spectra of Rita rita (PDF 1378 kb)
10695_2015_46_MOESM2_ESM.xlsx (117 kb)
ESM_2 The homology of mapped peptides with other species used for identification, the amino acid sequences of identified peptides, i.e., Hsp90 sequence from LC-MS/MS (XLSX 117 kb)
10695_2015_46_MOESM3_ESM.xlsx (192 kb)
ESM_3 The homology of mapped peptides with other species used for identification, the amino acid sequences of identified peptides, i.e., α-actinin sequence from LC-MS/MS (XLSX 192 kb)

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Copyright information

© Springer Science+Business Media Dordrecht 2015

Authors and Affiliations

  • Bimal Prasanna Mohanty
    • 1
  • Tandrima Mitra
    • 1
  • Sudeshna Banerjee
    • 1
  • Soma Bhattacharjee
    • 1
  • Arabinda Mahanty
    • 1
  • Satabdi Ganguly
    • 1
  • Gopal Krishna Purohit
    • 2
  • Dhanasekar Karunakaran
    • 1
  • Sasmita Mohanty
    • 2
  1. 1.Proteomics Unit, Biochemistry Laboratory, Fishery Resource and Environmental Management DivisionICAR-Central Inland Fisheries Research InstituteBarrackpore, KolkataIndia
  2. 2.KIIT School of BiotechnologyKIIT UniversityBhubaneswarIndia

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