Studies on the low molecular weight protein components in rabbit skeletal myosin

Gaetjens, Eric; Bárány, Kate; Bailin, Gary; Oppenheimer, Hans; Bárány, Michael

doi:10.1016/0003-9861(68)90106-9

Cited by 62 publications

(17 citation statements)

References 25 publications

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“…The antigen for the antiserum to total light chains (Fig- ure 2) was obtained by incubation of myosin at alkaline pH (Gaetjens et al, 1968). Myosin (~5 mg/ml) was exposed to pH 11, 0°, in the presence of 2 mM ATP, 0.1 M KC1, 1 mM dithiothreitol, 2 M LiCl, and 0.1 M glycine buffer for about 30 min.…”

Section: Methodsmentioning

confidence: 99%

Immunological approach to the role of the low-molecular-weight subunits in myosin. I. Physical-chemical and immunological characterization of the light chains

Holt¹,

Lowey²

1975

Biochemistry

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The light chains of chicken breast muscle myosin (alkali 1 and 2, 5,5'-dithiobis(2-nitrobenzoic acid) (DTNB) 1.c.) have been isolated in pure form and characterized with respect to amino acid composition, uv and circular dichroism (CD) spectral properties, and molecular weight. Antibodies specific for each of the light chains have been used to demonstrate the similarity of alkali 1 and 2 (mol wt 21,000 and 16,000, respectively), and the distinctness of these from DTNB 1.c. (mol wt of 18,000). The DTNB 1.c. isolated by a variety of methods were all immunologically identical. Significant cross-reactivity was observed between corresponding rabbit and chicken light chains, confirming other indications of homology between these proteins in the two species. The immunological difference between alkali 1 and 2 was largely accounted for by an N-terminal peptide, rich in proline, alanine, and lysine, which is unique to alkali 1. The presence of antibodies to this peptide in anti-alkali 1 serum suggests an immunological approach to the question of how alkali 1.c. are distributed in myosin.

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Section: Methodsmentioning

confidence: 99%

Immunological approach to the role of the low-molecular-weight subunits in myosin. I. Physical-chemical and immunological characterization of the light chains

Holt¹,

Lowey²

1975

Biochemistry

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“…Further purification of myosin was achieved by low ionic strength precipitation and ammonium sulfate fractionation (16). The purified myosin was separated into its heavy and light chain components according to the carbonate-citrate method (17).…”

Section: A T E R I a L S A N D M E T H O D Smentioning

confidence: 99%

Nonuniform Rates of Turnover of Myofibrillar Proteins in Rat Diaphragm

Low

Goldberg

1973

The Journal of Cell Biology

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“…From electrophoretic and hydrodynamic studies Stracher and collaborators concluded that the myosin molecule contains three small units per molecule, although on hydrodynamic data alone Frederiksen & Holtzer (1968) suggested that there were two. From several studies (Gaetjens, Barany, Bailin, Oppenheimer & Barany, 1968;Locker & Hagyard, 1967Florini & Brivio, 1969) the electrophoretic behaviour appears complex and the number present variable. Removal of these components from myosin results in a loss of adenosine triphosphatase activity, but Gaetjens et at.…”

mentioning

confidence: 99%

An electrophoretic study of the low-molecular-weight components of myosin

Perrie

Perry

1970

Biochemical Journal

698

290

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1. The low-molecular-weight components of myosin freshly prepared by the standard procedure from adult rabbit skeletal muscle migrated as four main bands Ml(1), Ml(2), Ml(3) and Ml(4) on polyacrylamide-gel electrophoresis in 8m-urea. 2. The number of bands increased on storage. This change was accelerated by increasing the temperature and pH. 3. None of the bands had electrophoretic mobilities identical with those of the well-characterized proteins of the myofibril or with the sarcoplasmic proteins. 4. By varying the ionic conditions and concentration of muscle mince used for the initial extraction it was possible to change the relative proportions of the two electrophoretic bands of intermediate mobility, Ml(2) and Ml(3). 5. The four-band picture similar to that obtained with rabbit was observed with myosin isolated from skeletal muscle of the rat, mouse, hamster, pigeon and chicken. 6. Rabbit cardiac myosin gave only two bands on electrophoresis. Myosin from rabbit red muscle gave a pattern intermediate between cardiac and white-skeletal-muscle myosin, i.e. the two fastest bands were present in decreased relative amounts. 7. It is suggested that the differences in the low-molecular-weight components of myosin from different types of muscle are a consequence of differences in the isoenzyme composition of the myosins.

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Studies on the low molecular weight protein components in rabbit skeletal myosin

Cited by 62 publications

References 25 publications

Immunological approach to the role of the low-molecular-weight subunits in myosin. I. Physical-chemical and immunological characterization of the light chains

Immunological approach to the role of the low-molecular-weight subunits in myosin. I. Physical-chemical and immunological characterization of the light chains

Nonuniform Rates of Turnover of Myofibrillar Proteins in Rat Diaphragm

An electrophoretic study of the low-molecular-weight components of myosin

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