Immunochemical evidence for the species-specificity of mammalian cardiac myosin and heavy meromyosin

Schwartz, Ketty; Bouveret, P.; Sébag, C; Leger, Jocelyne; Swynghedauw, Bernard

doi:10.1016/0005-2795(77)90236-7

Cited by 31 publications

(13 citation statements)

References 26 publications

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“…The antisera to native heavy meromyosin used were characterized in earlier papers [3,31]. Antisera to rabbit white skeletal and rat ventricular denatured heavy meromyosins were elicited in guinea-pigs, according to a schedule previously reported [25].…”

Section: Immunological Methodsmentioning

confidence: 99%

“…Cardiac myosins were extracted from the ventricles or atria dissected free from the great vessels. All muscles were frozen in liquid nitrogen immediately after excision and stored at -20 "C. Myosins were prepared either by slightly changing the procedure described by Weber and Portzehl [3,27] or according to Offer et al [28]. Heavy meromyosins were prepared and purified by Sepharose 6B chromatography as previously described [3].…”

Section: Preparation Of Myosins and Heavy Meromyosinsmentioning

confidence: 99%

“…x 200 mm) in the presence of 0.1 sodium dodecylsulfate, 0.082 M Tris and 0.4 M boric acid pH 7.1, at 40 mA/gel [3]. Relative molecular masses (M,) were derived from dodecylsulfate electrophoretic mobility measurements [29].…”

Section: Analytical Proceduresmentioning

confidence: 99%

“…In the heart, up to six different isoenzymes were described in 1978 in the same animal species [1,2], in addition to the phylogenic differences [3]. Besides the well-established differences between fast and slow isoenzymes, recent immunological observations made on skeletal muscle fibers strongly suggest that myosins from fast white and fast red fibers also differ [4].…”

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confidence: 99%

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Use of Antibodies against Dodecylsulfate-Denatured Heavy Meromyosins to Probe Structural Differences between Muscular Myosin Isoenzymes

et al. 1980

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Heavy meromyosin, a tryptic myosin fragment, was purified from rabbit fast twitch muscles and rat cardiac ventricles. Both types of heavy meromyosin were denatured by sodium dodecylsulfate and used to immunize guinea‐pigs after chromatography on Sephadex G‐10 to remove excess dodecylsulfate. Micro‐complement fixation analysis showed that the antisera were specific to a denatured configuration of heavy meromyosin and myosin, and hardly recognized the native proteins. Crossreactions performed with both rabbit skeletal and rat cardiac antisera indicated that the antigenic structures of denatured myosins varied according both to species (man, rabbit, rat or mouse), and to muscle‐type (red skeletal slow twitch, white skeletal fast twitch, cardiac atria or cardiac ventricles). Denatured heavy meromyosin chromatography on Sephadex G‐200 in the presence of 0.1% sodium dodecylsulfate enabled separation of several polypeptides groups. Of these, a polypeptide of M, 29000 was the most reactive and exhibited the same immunological specificities as the whole myosin molecule. The use of antibodies against denatured heavy meromyosin in conjunction with micro‐complement fixation therefore provides a discriminant means, not only for estimating the structural relationship between several myosin isoenzymes, but also for localizing constant and variable regions in the heavy chains of these isoenzymes.

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Section: Immunological Methodsmentioning

confidence: 99%

Section: Preparation Of Myosins and Heavy Meromyosinsmentioning

confidence: 99%

Section: Analytical Proceduresmentioning

confidence: 99%

mentioning

confidence: 99%

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Use of Antibodies against Dodecylsulfate-Denatured Heavy Meromyosins to Probe Structural Differences between Muscular Myosin Isoenzymes

et al. 1980

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“…wt 9000, isolated, respectively, from the heavy chains of rabbit skeletal muscle myosin and of bovine cardiac myosin, have been sequenced and compared [4,5]. Other information on the structure of myosin heavy chains has been obtained after chemical cleavage at specific residues [2,6-81, after limited enzymatic hydrolysis [2,3], or using an immunological approach [9]. The above studies concern the whole myosin or intact heavy chains isolated from different muscles or from the same muscle in different pathological states.…”

Section: Introductionmentioning

confidence: 99%