Electrophoretic analyses of atrial and ventricular cardiac myosins from foetal and adult rabbits

Srihari, Thota; Tuchschmid, C. R.; Hirzel, H; Schaub, Marcus C.

doi:10.1016/0305-0491(82)90212-7

Cited by 9 publications

(12 citation statements)

References 18 publications

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“…For calculation of the stoichiometry the chemical molecular weights of 21 000 dalton for LC,, 18000 for LC 2 and 66 000 for tropomyosin from both atrial and ventricular tissues were taken. This needs to be mentioned for the apparent molecular weights of the LC in SDS gel electrophoresis are different: 27400 dalton for LC, and 22600 for LC 2 from atrium and 26000 dalton for LC, and 21000 for LC 2 from ventricle' 22 '. The myosin HC and sometimes also actin were not reliably resolved in the isoelectrofocusing run and could therefore not be quantified.…”

Section: Methodsmentioning

confidence: 99%

Myosin isoenzymes in human hypertrophic hearts. Shift in atrial myosin heavy chains and in ventricular myosin light chains

Schaub

Tuchschmid

Srihari

et al. 1984

European Heart Journal

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Section: Methodsmentioning

confidence: 99%

Myosin isoenzymes in human hypertrophic hearts. Shift in atrial myosin heavy chains and in ventricular myosin light chains

Schaub

Tuchschmid

Srihari

et al. 1984

European Heart Journal

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“…By these techniques it was found that atrial and ventricular light chains are significantly different in various mammalian species so far investigated (16,18). It consists of two heavy chains and four light chains which appear to vary in different skeletal and cardiac muscles.…”

Section: Introductionmentioning

confidence: 99%

Isoforms of heavy and light chains of cardiac myosins from rat and rabbit

1982

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The light chains of myosin from atrial and ventricular tissues from rat and rabbit were examined by one- and two-dimensional polyacrylamide gel electrophoresis. The myosin heavy chains were electrophoretically isolated, digested after denaturation in sodium dodecyl sulfate with papain and proteinase from S. aureus V8, and the resulting peptides resolved in one-dimensional gel electrophoresis. The peptide patterns of myosin heavy chains from atrial and ventricular tissues of adult rabbits were different, indicating differences in their primary structures. No such differences could be detected in a total of around 180 peptides produced by the two proteinases from the myosin heavy chains of adult rat atrial and ventricular tissues. With regard to light chains, the same migration pattern was observed for atrial and ventricular tissues from both rat and rabbit. The atrial light chains ALC1 and ALC2 migrated with molecular weights lying between those of the ventricular light chains VLC1 and VLC2. In two-dimensional electrophoresis, the corresponding light chains from rat and rabbit co-migrated. An additional light chain was observed in foetal ventricles, which exhibited identical electrophoretic properties to ALC1 from adult atrial tissues. In rat myofibrillar preparations from atrium and ventricle, an unidentified protein (x) occurred in the region of light chain-1 but with a more acidic isoelectric point, which seems to be related to the developmental stage of these tissues and which could not be detected in rabbit heart tissues or in any skeletal muscles.

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“…Atrial and the ventricular free walls of mammalian hearts have different light chain compositions (13,15,19,21,25). However, no such differences have been observed between the left and right atria as well as between the left and right ventricles (21).…”

Section: Discussionmentioning

confidence: 94%

“…Most atrial myosin differs from ventricular myosin in both heavy and light chain composition (4,8,13,15,(19)(20)(21)25). The Ca2+-activated ATPase activity of atrial myosin exceeds that of ventricular myosin (8,13,21,26).…”

Section: Introductionmentioning

confidence: 96%

Myosin light chain compositions of the interatrial and interventricular septa of sheep heart

1985

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The myosin light chain composition of sheep interatrial and interventricular septa were analysed by one- and two-dimensional polyacrylamide gel. The interventricular septum has myosin light chain composition indistinguishable from that of ventricular myosin. Myosin from the interatrial septum contains three light chains, two of which co-migrated with the two atrial light chains (ALC1 and ALC2), while the third co-migrated with ventricular light chain 2 (VLC2). ALC1 are more abundant than ALC2 or VLC2 suggesting a mixed myosin population. Myosin with ALC1 and VLC2 light chain composition may be present, and its possible relationship with cardiac "conducting" cells is discussed.

show abstract

Electrophoretic analyses of atrial and ventricular cardiac myosins from foetal and adult rabbits

Cited by 9 publications

References 18 publications

Myosin isoenzymes in human hypertrophic hearts. Shift in atrial myosin heavy chains and in ventricular myosin light chains

Myosin isoenzymes in human hypertrophic hearts. Shift in atrial myosin heavy chains and in ventricular myosin light chains

Isoforms of heavy and light chains of cardiac myosins from rat and rabbit

Myosin light chain compositions of the interatrial and interventricular septa of sheep heart

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