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Acta Crystallographica Section F: Structural Biology and Crystallization Communications (1)
PLoS ONE (1)
Santi-Gadelha, Tatiane (2)
de Almeida Gadelha, Carlos Alberto (2)
Beltrão-Filho, Edvaldo Mesquita (1)
Cajazeiras, João Batista (1)
Canduri, Fernanda (1)
Cavada, Benildo S. (1)
Delatorre, Plínio (1)
Franco, Octavio Luiz (1)
Freitas, Beatriz Tupinamba (1)
Magnani, Marciane (1)
Moreno, Frederico Bruno Mendes Batista (1)
Rustiguel, Joane Kathelen Rodrigues (1)
Vasconcelos, Gracy Kelly Vieira (1)
da Costa, Whyara Karoline Almeida (1)
da Rocha, Bruno Anderson M. (1)
de Azevedo, Walter Filgueira (1)
de Souza, Evandro Leite (1)
Year of Publication
Comparative Protein Composition Analysis of Goat Milk Produced by the Alpine and Saanen Breeds in Northeastern Brazil and Related Antibacterial Activities
da Costa, Whyara Karoline Almeida
de Souza, Evandro Leite
Beltrão-Filho, Edvaldo Mesquita
Vasconcelos, Gracy Kelly Vieira
Franco, Octavio Luiz
The protein composition of goat milk differs between goat breeds and could present regional trends. The aim of this study was to comparatively analyze the protein composition of goat milk produced by the Alpine and Saanen breeds in northeastern Brazil and to evaluate the antibacterial activity of its protein fractions. SDS-PAGE, 2-DE electrophoresis and RP-HPLC analyses revealed the absence of αs1-casein in the milk of both breeds and no differences between the αs2-casein, β-casein, β-lactoglobulin and α-lactalbumin profiles. The amounts of soluble proteins and β-casein hydrolysis residues were higher in Saanen milk. Only the protein fraction containing the largest amounts of casein (F60–90%) inhibited bacterial growth, with MIC values between 50 and 100 mg/mL. This study describe for the first time three important points about the goat milk protein of two Brazilian goat breeders: absence of α-s1 casein in the protein profile, differences between the milk protein composition produced by goats of Alpine and Saanen breeders and antibacterial activity of unbroken proteins (casein-rich fraction) present in these milk.
Crystallization and preliminary X-ray diffraction analysis of a lectin from Canavalia maritima seeds
Moreno, Frederico Bruno Mendes Batista
Cajazeiras, João Batista
da Rocha, Bruno Anderson M.
Rustiguel, Joane Kathelen Rodrigues
Freitas, Beatriz Tupinamba
de Azevedo, Walter Filgueira
Cavada, Benildo S.
Acta Crystallographica Section F: Structural Biology and Crystallization Communications
A lectin from C. maritima was crystallized using the vapour-diffusion method and crystals diffracted to 2.1 Å resolution. A molecular-replacement search found a solution with a correlation coefficient of 69.2% and an R factor of 42.5%, refinement is in progress.
A lectin from Canavalia maritima seeds (ConM) was purified and submitted to crystallization experiments. The best crystals were obtained using the vapour-diffusion method at a constant temperature of 293 K and grew in 7 d. A complete structural data set was collected to 2.1 Å resolution using a synchrotron-radiation source. The ConM crystal belongs to the orthorhombic space group P21212, with unit-cell parameters a = 67.15, b = 70.90, c = 97.37 Å. A molecular-replacement search found a solution with a correlation coefficient of 69.2% and an R factor of 42.5%. Crystallographic refinement is under way.
lectins; Canavalia maritima
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