Cecile Gosselin-Rey

Parvalbumins from frog skeletal muscle (Rana Temporaria L.) Isolation and characterization Structural modifications associated with calcium binding

Two parvalbumins have been isolated from the skeletal muscle of Rana temporaria L. Amino acid composition, tryptic peptide maps, isoelectric points, calcium content and ultraviolet as well as circular dichroism spectra have been determined. Investigation on antigenic properties revealed no antigenic determinants common to both components. The two protein molecules appear to belong to far related gene lineages. They are also different from the parvalbumins found in Rana esculenta muscle. Modifications of physical parameters, associated with calcium binding and dissociation are described. While antigenicity remained essentially unchanged, conformational changes were revealed by alterations of circular dichroism spectra.

Polymorphism of parvalbumins and tissue distribution: characterization of component I, isolated from red muscles of Cyprinus carpio L.

The component I isolated from carp red muscle has been characterized as a true parvalbumin, fairly different from carp parvalbumins described so far. The protein is antigenically related to the parvalbumin III from pike, which belongs to the so called parvalbumin lineage alpha. Immunological investigations on the location of the various carp parvalbumins reveal genuine variation in the pattern of these proteins according to organ and type of muscular tissue.

Conformation and immunochemistry of parvalbumin III from Pike white muscle: Modification of the arginine residue with 1,2-cyclohexanedione

Abstract 1. 1. The single arginine residue of parvalbumin III from Pike white muscle has been modified with 1,2-cyclohexanedione. The purity of the modified protein is established by amino acid analysis, immunoelectrophoresis and peptide mapping. 2. 2. The immunochemical study indicates the loss of at least two antigenic determinants together with conformational changes in the molecule. 3. 3. A reduced percentage of α helicity is demonstrated by ORD and CD measurements. 4. 4. The Ca2+ associated with the modified protein is reduced to 50-25% of the amount in the native parvalbumin. 5. 5. It is concluded that the arginine residue plays a key role in the tertiary structure of the molecule.

Parvalbumins distribution and physical state inside the muscle cell

Single skinned muscle fibres (frog) have been submitted to double Ouchterlony immunodiffusion assays with antibodies directed against the two species of frog parvalbumins. The antigenic material which diffuses out of each fibre contains the two parvalbumins. Their presence in each cell is thus demonstrated. The amount of parvalbumins having diffused out of the fibre has been quantified. It corresponds to the parvalbumin content of the cell. This implies that these proteins are freely soluble in the muscle sarcoplasm.

Isolation and molecular properties of creatine kinase from carp white muscle

Abstract 1. 1. Three creatine kinase isoenzymes analogous to the MM, MB and BB forms of enzyme in higher vertebrates, are present in adult carp skeletal muscles, heart and brain. 2. 2. A procedure is described to isolate the MM isoenzyme from carp white muscle. Purity of the enzyme preparations is established from starch gel electrophoresis and ultracentrifugation analysis. 3. 3. A 6-fold purification yields pure enzyme with low catalytic activity compared to that of rabbit muscle enzyme. The validity and implications of this finding are discussed. 4. 4. The molecular weight, diffusion and sedimentation coefficients as well as amino acid composition of carp MM creatine kinase have been determined. 5. 5. Peptide maps of the rabbit and carp MM enzymes are compared. As a first approximation, a maximum of 75% similarity in peptides may be expected. 6. 6. Eight cysteine residues are found on amino acid analysis, two of which are essential to catalytic activity.

Amino acid analysis and peptide mapping of bovine carotid actin

Abstract Actin from bovine carotid is found to be essentially similar to actins extracted from other muscular tissues, as demonstrated by amino acid analysis and peptide mapping. So far no difference in molecular structure has been detected which could account for the unusual incomplete depolymerization of this actin. 3-Methylhistidine is present at a ratio of 1 per 8 histidines, similar to that found in rabbit actin. This ratio tends to indicate that the molecular weight of actin monomer from smooth and striated muscle is near 48 000, instead of the previously accepted value of 60 000.

Immunological cross-reactions among cyprinidae parvalbumins

Abstract The parvalbumin pattern in white muscle from seven Cyprinidae has been determined by starch gel electrophoresis analysis. The immunochemical discrimination of the various components using several monospecific antisera against a number of distinct Cyprinidae parvalbumins has been qualitatively evaluated by immunoelectrophoresis. The results show that immunologically different groups of parvalbumins can be distinguished within these patterns. One of these groups includes at least one component which is present in each of the seven species investigated. A similar component has been found in a species of Siluridae which, like the Cyprinidae, belongs to the well defined systematic superorder of the Ostariophysi.

Immunological cross-reactions among gadidae parvalbumins

Abstract Antisera raised against apparently homogeneous whiting parvalbumin III have been found to recognize two non cross-reacting molecular species of parvalbumins. Aliquots of these antisera have been separately absorbed with two distinct parvalbumins from a near-related fish species, namely haddock parvalbumins II and III, and also with the homologous antigen. The immunochemical reactivities of absorbed and non-absorbed antisera toward parvalbumins from nine Gadidae species have been systematically explored by immunoelectrophoresis. The observed cross-reactions lead to distinguish two groups among Gadidae parvalbumins. So far this discrimination can be correlated with differences in amino-acid compositions, peptide maps and sequences which are known to characterize several protein members from each of the two groups. Using the same anti-whiting antisera, a tenuous common antigenic reactivity is shown between Gadidae and some Cyprinidae parvalbumins.