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Identification of myosin heavy chain isoforms in skeletal muscle of four Southern African wild ruminants.
Comp Biochem Physiol A Mol Integr Physiol. 2007 Oct; 148(2):399-407.CB

Abstract

The aim was to separate and characterize the myosin heavy chain (MHC) isoforms of four southern African wild ruminants, namely Blesbuck (Damaliscus dorcas phillipsi), Kudu (Tragelaphus strepsiceros), Black Wildebeest (Connochaetes gnou) and Blue Wildebeest (Connochaetes taurinus). Longissimus dorsi muscle samples were subjected to SDS-PAGE and Western blot analyses using antibodies raised against MHC isoforms. The specificity of these antibodies was assessed using immunohistochemistry combined with ATPase histochemistry, Three MHC isoforms were separated and the bands were identified from fastest to slowest migrating as MHC I, MHC IIx and MHC IIa. The mobility of the MHC isoforms was similar for all four species, including that of bovine, but differed from human muscle. Kudu muscle exhibited the lowest proportion of MHC I and the highest proportion of MHC IIx, whereas Blesbuck muscle had the least MHC IIx. The two Wildebeest species were intermediate in isoform content. In conclusion, when new species are studied, existing electrophoretic protocols may need to be modified to achieve quantifiable separation and isoform migration pattern must be verified in order to reach correct interpretations. Furthermore, antibody specificity may differ between techniques as well as species and needs confirmation.

Authors+Show Affiliations

Department of Physiological Sciences, University of Stellenbosch, Private Bag X1, Matieland, 7602, South Africa.No affiliation info availableNo affiliation info available

Pub Type(s)

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

Language

eng

PubMed ID

17631404

Citation

Kohn, Tertius A., et al. "Identification of Myosin Heavy Chain Isoforms in Skeletal Muscle of Four Southern African Wild Ruminants." Comparative Biochemistry and Physiology. Part A, Molecular & Integrative Physiology, vol. 148, no. 2, 2007, pp. 399-407.
Kohn TA, Hoffman LC, Myburgh KH. Identification of myosin heavy chain isoforms in skeletal muscle of four Southern African wild ruminants. Comp Biochem Physiol A Mol Integr Physiol. 2007;148(2):399-407.
Kohn, T. A., Hoffman, L. C., & Myburgh, K. H. (2007). Identification of myosin heavy chain isoforms in skeletal muscle of four Southern African wild ruminants. Comparative Biochemistry and Physiology. Part A, Molecular & Integrative Physiology, 148(2), 399-407.
Kohn TA, Hoffman LC, Myburgh KH. Identification of Myosin Heavy Chain Isoforms in Skeletal Muscle of Four Southern African Wild Ruminants. Comp Biochem Physiol A Mol Integr Physiol. 2007;148(2):399-407. PubMed PMID: 17631404.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Identification of myosin heavy chain isoforms in skeletal muscle of four Southern African wild ruminants. AU - Kohn,Tertius A, AU - Hoffman,Louw C, AU - Myburgh,Kathryn H, Y1 - 2007/06/14/ PY - 2006/10/31/received PY - 2007/05/26/revised PY - 2007/05/29/accepted PY - 2007/7/17/pubmed PY - 2007/10/20/medline PY - 2007/7/17/entrez SP - 399 EP - 407 JF - Comparative biochemistry and physiology. Part A, Molecular & integrative physiology JO - Comp Biochem Physiol A Mol Integr Physiol VL - 148 IS - 2 N2 - The aim was to separate and characterize the myosin heavy chain (MHC) isoforms of four southern African wild ruminants, namely Blesbuck (Damaliscus dorcas phillipsi), Kudu (Tragelaphus strepsiceros), Black Wildebeest (Connochaetes gnou) and Blue Wildebeest (Connochaetes taurinus). Longissimus dorsi muscle samples were subjected to SDS-PAGE and Western blot analyses using antibodies raised against MHC isoforms. The specificity of these antibodies was assessed using immunohistochemistry combined with ATPase histochemistry, Three MHC isoforms were separated and the bands were identified from fastest to slowest migrating as MHC I, MHC IIx and MHC IIa. The mobility of the MHC isoforms was similar for all four species, including that of bovine, but differed from human muscle. Kudu muscle exhibited the lowest proportion of MHC I and the highest proportion of MHC IIx, whereas Blesbuck muscle had the least MHC IIx. The two Wildebeest species were intermediate in isoform content. In conclusion, when new species are studied, existing electrophoretic protocols may need to be modified to achieve quantifiable separation and isoform migration pattern must be verified in order to reach correct interpretations. Furthermore, antibody specificity may differ between techniques as well as species and needs confirmation. SN - 1095-6433 UR - https://www.unboundmedicine.com/medline/citation/17631404/Identification_of_myosin_heavy_chain_isoforms_in_skeletal_muscle_of_four_Southern_African_wild_ruminants_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S1095-6433(07)01052-5 DB - PRIME DP - Unbound Medicine ER -