NISCAIR Online Periodicals Repository

Research Journals >
Indian Journal of Biochemistry and Biophysics (IJBB) >
IJBB Vol.43 [2006] >
IJBB Vol.43(4) [August 2006] >

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
Muscle-type specificity
MyHC isoforms/isomers
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.
Page(s): 217-225
ISSN: 0301-1208
Source:IJBB Vol.43(4) [August 2006]

Files in This Item:

File Description SizeFormat
IJBB 43(4) 217-225.pdf1.25 MBAdobe PDFView/Open
 Current Page Visits: 89 
Recommend this item


Online Submission of Articles |  NISCAIR Website |  National Knowledge Resources Consortium |  Contact us |  Feedback

Disclaimer: NISCAIR assumes no responsibility for the statements and opinions advanced by contributors. The editorial staff in its work of examining papers received for publication is helped, in an honorary capacity, by many distinguished engineers and scientists.

CC License Except where otherwise noted, the Articles on this site are licensed under Creative Commons License: CC Attribution-Noncommercial-No Derivative Works 2.5 India

Copyright © 2015 The Council of Scientific and Industrial Research, New Delhi. All rights reserved.

Powered by DSpace Copyright © 2002-2007 MIT and Hewlett-Packard | Compliant to OAI-PMH V 2.0

Home Page Total Visits: 171579 since 01-Sep-2015  Last updated on 30-Jun-2016Webmaster: