Parvalbumins
Mostrando 1-5 de 5 artigos, teses e dissertações.
-
1. Estudo da imunorreatividade das proteínas ligantes de cálcio na neuroquímica da medula espinal de ratos submetidos à atividade física espotânea na roda de corrida. / Study of the imunoreativite of ligantes calcium proteins in the neurochemistry of the espinal marrow of submitted rats the spontaneous physical activity in the race wheel
Actions of the physical activity in the neurochemistry focuzing calcium-bindin proteins and the activation of the glial cells in the spinal cord of the rat were investigated with imunohistochemistry over. Male wistar adult rats were divided in two groups: trained, which animals exercised in the wheel running for 4 and 14 nigths; and sedentary, which animals
Publicado em: 2008
-
2. A Phosphate-Acceptor Protein Related to Parvalbumins in Dogfish Skeletal Muscle
A phosphate-acceptor protein was isolated from the skeletal muscle of the Pacific dogfish (Squalus acanthias) displaying properties extremely similar to those of the parvalbumins, i.e., the low-molecular-weight, soluble, Ca-binding muscle proteins found in fish and amphibians. It has the same characteristic UV spectrum, strong affinity for calcium, and immun
-
3. Amino-acid sequence of parvalbumin from rabbit skeletal muscle.
Determination of the complete amino-acid sequence of rabbit skeletal muscle parvalbumin is described. The sequence of 86 of the 109 total residues was determined automatically by sequenator analyses of peptides obtained after cleavage with CNBr or with trypsin. The positions of the remaining 23 residues were determined by subtractive Edman degradation of try
-
4. Tritium planigraphy: From the accessible surface to the spatial structure of a protein
The method of tritium planigraphy, which provides comprehensive information on the accessible surface of macromolecules, allows an attempt at reconstructing the three-dimensional structure of a protein from the experimental data on residue accessibility for labeling. The semiempirical algorithm proposed for globular proteins involves (i) predicting theoretic
The National Academy of Sciences.
-
5. Structure of a Calcium-Binding Carp Myogen
The amino-acid sequence and three-dimensional structure of a calcium-binding protein prepared from carp muscle has been determined. This protein, designated carp-muscle calcium-binding protein B, is one of three closely related parvalbumins found in this tissue. The electron density map, calculated by heavyatom substitution crystallographic methods to 2.0-Å