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Correlation between biochemical properties and adaptive diversity of skeletal muscle myofibrils and myosin of some air-breathing teleosts.
Indian J Biochem Biophys. 2006 Aug; 43(4):217-25.IJ

Abstract

Functional properties of myofibrils and relative stability of myosin of five teleosts Channa punctata, Clarias batrachus, M astacembalus 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 a-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. armnatus 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.

Authors+Show Affiliations

Laboratory of Biochemical Genetics, Department of Zoology, Aligarh Muslim University, Aligarh 202 002, India.No affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

17133765

Citation

Ahmad, Riaz, and Absar-ul Hasnain. "Correlation Between Biochemical Properties and Adaptive Diversity of Skeletal Muscle Myofibrils and Myosin of some Air-breathing Teleosts." Indian Journal of Biochemistry & Biophysics, vol. 43, no. 4, 2006, pp. 217-25.
Ahmad R, Hasnain AU. Correlation between biochemical properties and adaptive diversity of skeletal muscle myofibrils and myosin of some air-breathing teleosts. Indian J Biochem Biophys. 2006;43(4):217-25.
Ahmad, R., & Hasnain, A. U. (2006). Correlation between biochemical properties and adaptive diversity of skeletal muscle myofibrils and myosin of some air-breathing teleosts. Indian Journal of Biochemistry & Biophysics, 43(4), 217-25.
Ahmad R, Hasnain AU. Correlation Between Biochemical Properties and Adaptive Diversity of Skeletal Muscle Myofibrils and Myosin of some Air-breathing Teleosts. Indian J Biochem Biophys. 2006;43(4):217-25. PubMed PMID: 17133765.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Correlation between biochemical properties and adaptive diversity of skeletal muscle myofibrils and myosin of some air-breathing teleosts. AU - Ahmad,Riaz, AU - Hasnain,Absar-ul, PY - 2006/12/1/pubmed PY - 2007/1/12/medline PY - 2006/12/1/entrez SP - 217 EP - 25 JF - Indian journal of biochemistry & biophysics JO - Indian J Biochem Biophys VL - 43 IS - 4 N2 - Functional properties of myofibrils and relative stability of myosin of five teleosts Channa punctata, Clarias batrachus, M astacembalus 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 a-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. armnatus 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. SN - 0301-1208 UR - https://www.unboundmedicine.com/medline/citation/17133765/Correlation_between_biochemical_properties_and_adaptive_diversity_of_skeletal_muscle_myofibrils_and_myosin_of_some_air_breathing_teleosts_ DB - PRIME DP - Unbound Medicine ER -