Please use this identifier to cite or link to this item: http://nopr.niscair.res.in/handle/123456789/3290
Title: Correlation between biochemical properties and adaptive diversity of skeletal muscle myofibrils and myosin of some air-breathing teleosts
Authors: Ahmad, Riaz
Hasnain, Absar-ul
Keywords: Air-breathing teleosts
Chymotryptic Peptide maps
Difference spectra
Hydrophobic interactions
m-ATPase
Muscle-type specificity
MyHC isoforms/isomers
SDS-PAGE
Structural plasticity
Issue Date: Aug-2006
Publisher: CSIR
Abstract: Functional properties of myofibrils and relative stability of myosin of five teleosts Channa punctata, Clarias batrachus, Mastacembalus armatus, Labeo rohita and Catla catla adapted to different breathing modes were compared. Myofibrillar contractility and m-ATPase of air-breathing organ (ABO) possessing C. punctata and C. batrachus were low and least affected by pH in the range of 7.1-8.5. However, their myosin isoforms were relatively thermostable, more soluble at sub-neutral pH values, between 0.1 to 0.15 M KCl concentrations and less susceptible to α-chymotryptic digestion. In contrast, myofibrils and myosin of water-breather major carps L. rohita and C. catla were more contractile and susceptible to pH and salt concentrations. Thus, correlation between catalytic efficiency and relative stability of myofibrils and myosin of ABO-possessing teleosts was of reverse order and magnitude, as compared to water-breathers. Interestingly, myofibrils and myosin of the behavioral air-breather M. armatus showed intermediate properties. The specific levels of m-ATPase of all the five teleosts were in conformity with the levels of metabolic marker, the lactate dehydrogenase. The effect of chymotryptic cleavage of 94 and 173 kDa domains on ATPase, individuality of peptide maps of MyHC isomers and perturbation of phenylalanine residues by urea implicated hydrophobic residues in stabilizing myosin structure in these fish. The present study suggests two apparent evolutionary modifications of myofibrils and myosin in ABO-possessing teleosts: (i), ‘down-regulation’ of ATPase that explains sluggishness of such species and, (ii), more stable molecular structure to support stress of air-breathing modes of life.
Description: 217-225
URI: http://hdl.handle.net/123456789/3290
ISSN: 0301-1208
Appears in Collections:IJBB Vol.43(4) [August 2006]

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