COMPARATIVE ELECTROPHORETIC STUDIES OF LENS PROTEIN ISOLATED FROM PUNTIUS TICTO (HAMILTON 1822) AND RASBORA DANICONUS (HAMILTON 1822)

Authors

  • E. R. MARTIN
  • S. D. PAGARE

Keywords:

Lens protein, Crystallins, Insoluble proteins, P. ticto, R. daniconus

Abstract

A comparative electrophoretic study of the eyelens protein of two freshwater fishes viz. Puntius ticto and Rasbora
daniconus was carried out. Electrophoretic analyses revealed substantial differences in the polypeptide distribu-
tion in both the fishes. SDS-PAGE of water soluble fractions of lens protein showed several bands ranging from
70-13.5 kDa and 74-13.5 kDa in P. ticto and R. daniconus respectively. The insoluble protein fraction was further
resolved into the urea soluble lens protein (USLP) and plasma membrane protein fraction(PMP), SDS-PAGE
analysis of the USLP fraction showed the presence of 6 bands ranging from 120-13.5 kDa in P. ticto and 114- 13,5
kDa in R. daniconus The PMP fraction of P. ticto resolved into 6 subunits ranging from 74-13.5 kDa. In contrast
only two bands corresponding to 29 and 13.5 KDa was observed for the PMP fraction of R. daniconus . The
present study demonstrates a complete variation in the protein pattern of the soluble and insoluble protein
fraction in these two fishes. The variation in eye lens protein which are considered to be a conserved protein
suggest that the R. daniconus had undergone gene duplication in the course of evolution and the two fishes may
have evolved differently.

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Published

2012-10-25

How to Cite

E. R. MARTIN, & S. D. PAGARE. (2012). COMPARATIVE ELECTROPHORETIC STUDIES OF LENS PROTEIN ISOLATED FROM PUNTIUS TICTO (HAMILTON 1822) AND RASBORA DANICONUS (HAMILTON 1822). The Bioscan, 7(4), 571–574. Retrieved from https://thebioscan.com/index.php/pub/article/view/1094

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