Anne d’Albis

Université Paris-Sud

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Chantal Janmot

Institut de Biochimie et Biophysique Moléculaire et Cellulaire

R Couteaux

Institut Curie

Jean‐Jacques Béchet

Université Paris Cité

Jean‐Claude Mira

Université Paris Cité

Anne‐Marie Lompré

Fondation pour l’innovation en Cadiométabolisme et Nutrition

Walter Gratzer

King's College London

C. Pantaloni

Centre National de la Recherche Scientifique

Christophe Chanoine

Inserm

Janez Sketelj

University of Ljubljana

J C Mira

Université Paris Cité

Cooperative Institutions

Centre National de la Recherche Scientifique

Université Paris Cité

Inserm

Université Paris-Sud

Sorbonne Université

Institut de Biologie Physico-Chimique

Hôpital Lariboisière

Laboratoire de Biologie du Développement

Centre National pour la Recherche Scientifique et Technique (CNRST)

Université Paris-Saclay

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Myosin isoforms in mackerel (Scomber scombrus) red and white muscles

FEBS Letters (1989)

Iciar Martı́nez R. L. Olsen Ragni Ofstad Chantal Janmot Anne d’Albis

Myosin extracts of red and white muscles from mackerel ( Scomber scombrus ) were analyzed by native electrophoresis to investigate the existence of myosin isoforms in both kind of muscles, and by two‐dimensional and SDS gel electrophoresis to study their subunit composition. Two isoforms were found in red muscle comprising one type of heavy chain and two light chains. Four isoforms were found in white muscle made up of one type of heavy chain and three types of light chains. The heavy chains from white muscle showed a higher electrophoretic mobility than that of red muscle in SDS‐PAGE. Both heavy chains had an intermediate mobility between those of slow and fast myosins from rat diaphragm.

Scomber

White (mutation)

10.1016/0014-5793(89)80891-9

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Citations (25)

Observations of interactions between myofibrillar proteins by chemical cross‐linking

FEBS Letters (1975)

Anne d’Albis

10.1016/0014-5793(75)80269-9

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Citations (3)

Regulation by thyroid hormones of terminal differentiation in the skeletal dorsal muscle

Developmental Biology (1987)

Christophe Chanoine Anne d’Albis Michele Lenfant-Guyot Chantal Janmot Claude L. Gallien

Myofibril

10.1016/0012-1606(87)90424-6

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Citations (32)

Optical Spectroscopic Study of the ADP‐Myosin Interaction

European Journal of Biochemistry (1978)

David J. Marsh Anne d’Albis Walter Gratzer

The binding of ADP to heavy meromyosin, and the separated subfragment 1 components S-1(A1) and S-1 (A2), has been observed by ultraviolet spectrophotometry. The results are compatible with the presence of spectroscopically equivalent and independent sites, one per head, at both 10 degrees C and 25 degrees C. We do not observe the heterogeneity of binding and of the spectroscopic response that has been reported. The binding has also been followed by other methods sensitive to the effect of ligand on the aromatic residues of the protein, viz. intrinsic fluorescence of heavy meromyosin and changes in the near-ultraviolet Cotton effects of myosin, and its active fragments. Within the limits of our experimental precision, the binding profiles, based on concentration of myosin heads, are the same for myosin as for subfragment 1. A perturbation in the circular dichroism is also generated by pyrophosphate, which competes with ADP. The spectra suggest that subsites for the purine ring and the diphosphate can be recognized. The sensitivity of binding profiles obtained by methods of the kind used here to cooperative or antagonistic interactions between the binding sites has been analysed. It is clear that sizeable effects of this nature could be concealed by the binding curves, even for high experimental precision.

Heavy meromyosin

Adenosine diphosphate

10.1111/j.1432-1033.1978.tb12014.x

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Citations (17)

Binding of competitive inhibitors to the different pH-dependent forms of trypsin

Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics (1969)

Jean‐Jacques Béchet Anne d’Albis

Benzamidine

Dissociation constant

Optical rotatory dispersion

Complex formation

10.1016/0005-2744(69)90225-3

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Citations (20)

Correlation among the proton charges and molecular masses of myosin subunits

FEBS Letters (1989)

Jean‐Jacques Béchet Anne d’Albis

The molecular masses and isoelectric points of myosin light and heavy chains were calculated from their known primary sequences and their respective distribution in a two‐dimensional graph is displayed. Implications for the electrophoretic study of myosin subunits are inferred from this analysis.

10.1016/0014-5793(89)80004-3

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Citations (10)

Note sur l'autoassociation de la trypsine a pH 4.8

Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics (1970)

Anne d’Albis

10.1016/0005-2795(70)90041-3

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Citations (3)

Base pairing of adenine and uracil derivatives in the presence of water

Biopolymers (1975)

Anne d’Albis Marvin Wickens Walter Gratzer

Abstract The association of chloroform‐soluble derivatives of uracil and adenine has been examined in chloroform solution in the presence of dissolved water. Analysis by infrared spectroscopy shows that complex formation still occurs in these conditions, and that the extent of association is substantially unchanged by the presence of water. Evidence is presented for the coexistence of two kinds of base pair (involving, respectively, the C 2 and C 4 carbonyl groups of the pyrimidine) in the solutions, and for some displacement in their relative balance by the added water. The binding of water to the C 2 and C 4 carbonyl groups can be separately observed in both the free uracil derivative and its 1:1 complex with 9‐ethyladenine. Little or no competition has been found to occur between the formation of base pairs and binding of water to the bases, as judged by measurements of water solubility in chloroform solutions of the bases individually and in 1:1 mixtures. The evidence suggests that this phenomenon can be largely explained by the formation of double hydrogen bonds by the uracil carbonyl groups. Taken together with recent published observations, the results indicate that hydrogen bonding may make a much greater energetic contribution to conformational stability of biopolymers in aqueous solution that has been supposed.

Uracil

Base (topology)

10.1002/bip.1975.360140709

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Citations (20)

Long-term changes in myosin heavy chain composition after botulinum toxin a injection into rat medial rectus muscle.

PubMed (2001)

Branka Stirn Kranjc Janez Sketelj Anne d’Albis Ida Eržen

To study long-term changes of extraocular muscles after botulinum toxin (Botx) A-induced paralysis, with special emphasis on myosin heavy chain (MyHC) isoform pattern in muscle fibers.Botx A (5 IU) was injected into the ocular medial rectus (MR) muscles of adult rats. After 1, 5, and 8 months muscle cross sections were examined immunohistochemically, histochemically, and morphometrically. MyHC content was analyzed by gel electrophoresis.Paralyzed MR muscles displayed mildly atrophic and hypertrophic muscle fibers and decreased oxidative metabolism, due to decreased succinate dehydrogenase activity. However, muscle morphology was not grossly disturbed. MyHC profile was shifted toward slower isoforms. Electrophoretic analysis showed that the share of MyHCI, and especially of MyHCIIa and MyHCIIx/d, increased several fold, whereas the share of MyHCIIb decreased heavily during the first 5 months. Immunohistochemical analysis generally mirrored the results obtained by electrophoresis. Moreover, specific extraocular MyHC isoform MyHCeom disappeared and could not be detected during the whole experimental period. The portion of MyHCIIb relatively increased 8 months after Botx A injection, although the MyHC profile was still far from normal.These long-lasting changes in Botx A-paralyzed ocular MR muscles most probably reflect their inability to regain their unique functional characteristics after new motor end plate formation and recovery of muscle contraction.

Medial rectus muscle

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Citations (53)

Electrophoretic examination of native myosin

FEBS Letters (1973)

Anne d’Albis Walter Gratzer

10.1016/0014-5793(73)80042-0

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Citations (41)