Electrophoretic separation of bovine muscle myosin heavy chain isoforms

Citation
B. Picard et al., Electrophoretic separation of bovine muscle myosin heavy chain isoforms, MEAT SCI, 53(1), 1999, pp. 1-7
Citations number
34
Categorie Soggetti
Food Science/Nutrition
Journal title
MEAT SCIENCE
ISSN journal
03091740 → ACNP
Volume
53
Issue
1
Year of publication
1999
Pages
1 - 7
Database
ISI
SICI code
0309-1740(199909)53:1<1:ESOBMM>2.0.ZU;2-N
Abstract
This study concerns the definition of the optimum conditions for separation of adult and developmental myosin heavy chain (MHC) isoforms in bovine mus cle. The various techniques published do not result in good separation of t he MKC in this species. The trials carried out concerned the concentration of acrylamide and N,N'-methylene-bis-acrylamide, and more particularly the concentration of Tris in the separating gel. The finding was that analysis of adult isoforms and developmental isoforms require different conditions. A acrylamide gradient of 3.5-10% with 200 mM Tris pH 8.8 gives good resolut ion for adult isoforms. Under these conditions 3 fast adult isoforms are re vealed. However, study of MHC isoforms throughout foetal life in bovines is complex, and requires the combined use of more than one gel (gradient 3.5- 10% at 200 mM Tris and gradient 3.5-10% at 250 mM Tris). (C) 1999 Elsevier Science Ltd. All rights reserved.