RESUMO
The marine sponge Anthosigmella varians contains proteins that agglutinate human erythrocytes irrespective of their ABO group antigens. The hemagglutination reaction depends on divalent cations and is not inhibited by L-arabinose, D-xylose, L-rhamnose, D-galactose, D-glucose, L and D-fucose, N-acetyl-D-galac-tosamine, N-acetyl-D-glucosamine, methyl-alpha-D-mannopiranoside, D-cellobiose, lactose, maltose, melibiose nor raffinose (33 mM each). A partial purification of the hemagglutinins with 31-fold increase in SA and 80% recovery of activity was obtained after gel filtration and ion-exchange gradient elution chromatography. Hemadsorption experiments carried out with the semipurified fraction using glutaraldehyde-fixed human erythrocytes suggest that proteins with molecular weight of 90 and 34 kDa participate in this reaction.
Assuntos
Hemaglutininas/análise , Poríferos/química , Animais , Brasil , Cromatografia por Troca Iônica , Hemadsorção , Peso Molecular , Água do MarRESUMO
The marine sponge Anthosigmella varians contains proteins that agglutinate human erythrocytes irrespective of their ABO group antigens. The hemagglutination reaction depends on divalent cations andf is not inhibited by L-arabinose, D-xylose, L-rhamnose, D-galactose, D-glucose, L and D-fucose, N-acetyl-D-galactosamine, N-acetyl-D-glucosamine, methyl-alpha-Dmannopiranoside, D-cellobiose, lactose, maltose, melibiose nor raffinose (33 mM each). A partial purification of the hemagglutinins with 31-fold ioncrease in SA and 80% recovery of activity was obtained after gel filtration and ion-exchange gradient elution chromatography. Hemadsorption experiments carried our with out with the semipurified fraction using glutaraldehyde-fixed human erythrocytes suggest that protein with molecular weight of 90 and 34 kDa participate in this rection
Assuntos
Animais , Hemaglutininas/análise , Poríferos/química , Brasil , Cátions Bivalentes , Cromatografia por Troca Iônica , Hemadsorção , Água do MarRESUMO
A mitogenic lectin for human lymphocytes is present in the marine sponge Desmapsama anchorata. The protein hemagglutinates red blood cells irrespective of ABO group antigens. We now report the isolation of this lectin, by affinity chromatography on a column of raffinose conjugated to epoxy-activated Sepharose 6B, in 8.3% yield and with a purification index of 27 based on hemagglutinating activity. The isolated lectin is a glycoprotein with two subunits with molecular weights of about 18 and 36 kDa which display carbohydrate combining sites of similar specificities and can be associated in different forms.
Assuntos
Cromatografia de Afinidade/métodos , Lectinas/isolamento & purificação , Poríferos/análise , Animais , Eletroforese em Gel de Poliacrilamida , HemaglutinaçãoRESUMO
A mitogenic lectin for human lymphocytes is present in the marine sponge Desmapsama anchorata. The protein hemagglutinates red blood cells irrespective of ABO group antigens. We now report the isolation of this lectin, by affinity chromatography on a column of raffinose conjugated to epoxy-activated Sepharose 6B, in 8.3% yield and with a purification index of 27 based on hemagglutinating activity. The isolated lectin is a glycoprotein with two subunits with molecular weights of about 18 and 36 kDa which display carbohydrate combining sites of similar specificities and can be associated in different forms
Assuntos
Cromatografia de Afinidade , Lectinas/isolamento & purificação , Poríferos/análise , Eletroforese em Gel de Poliacrilamida , HemaglutinaçãoRESUMO
1. A D-galactose-specific lectin was isolated from crude extracts of the marine sponge Cinachyrella alloclada by affinity chromatography on Sepharose 4B. 2. The lectin agglutinated human erythrocytes irrespective of their ABO group antigens. 3. Hemagglutination inhibition tests indicated that the lectin binds D-galactose or carbohydrates having a terminal nonreducing D-galactosyl group. 4. C. alloclada lectin was mitogenic for human peripheral blood lymphocytes when AB serum was omitted during the first 24 h of culture. 5. Human serum apparently contains substances which bind or inactivate this lectin.
Assuntos
Proteínas de Ligação ao Cálcio , Proteínas de Transporte/isolamento & purificação , Lectinas/isolamento & purificação , Proteínas de Transporte de Monossacarídeos , Proteínas Periplásmicas de Ligação , Poríferos/análise , Animais , Cromatografia de Afinidade , Eletroforese em Gel de Poliacrilamida , Eritrócitos/efeitos dos fármacos , HemaglutinaçãoRESUMO
1. A D-galactose-specific lectin was isolated from crude extracts of the marine sponge Cinachyrella alloclada by affinity chromatography on sepharose 4B. 2. The lectin agglutinated human erythrocytes irrespective of ther ABO group antigens. 3. Hemagglutination inhibition tests indicated that the lectin binds D-galactose or carbohydrates having a terminal nonreducing D-galactosyl group. 4. C. alloclada lectin was mitogenic for human periheral blood lymphocytes when AB serum was omitted during the first 24 h of culture. 5 Human serum apparently contains substances which bind or inactivate this lectin
