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Biomedical subjects

D Danon

Publications and source records attributed to D Danon.

At least 55 records · Page 3Linked to original sources
PubMed1976

Redistribution of surface anionic sites on the luminal front of blood vessel endothelium after interaction with polycationic ligand.

The ability of anionic groups on the luminal surface of blood vessels to redistribute by lateral migration under the influence of multivalent ligands was analyzed by electron microscopy, using cationized ferritin (CF). In vitro interaction of blood vessel segments with CF results in rapid aggregation of most anionic sites on the luminal fromt of the endothelium, followed by internalization or detachment of the CF patches, leaving most of the luminal surface devoid of anionic sites. Further incubation of such endothelial cells without CF results in regeneration of binding capacity for the polycationic label. Transport of CF, but not of native ferritin, across the endothelium by vesicle transport, followed by exocytosis of the interiorized CF clusters on the tissue front of the endothelium, was also observed. The possibility that such activities in the blood vessels in vivo may be associated with local changes in the normal distribution of the surface anionic sites as well as in accumulation of debris in the subendothelial layers of the vessels is suggested.

Animals↗
PubMed1976

Effect of serum from leukapheresed mice on myelocytes, promyelocytes and colony-forming cells.

Leukapheresis of neutrophil granulocytes in mice increased the myelopoietic activity of their serum. Leukapheresed mouse serum (LMS) caused a threefold increase in the in vitro stathmokinetic index of myeloid precursors. Five to ten minutes of incubation were sufficient to change the colony-forming capacity of mouse bone marrow cells as expressed by the increase in the ratio of granuloid to erythroid cells in spleen colonies. The in vitro stathmokinetic index assay also showed that there are diurnal variations in levels of granulopoietic activity in normal mouse sera. However, at any time of the day, LMS had higher granulopoietic activity.

Animals↗
PubMed1976

Comparison of the immune response potential of newborn mice to T-dependent and T-independent synthetic polypeptides.

Newborn mice do not, in general, produce antibodies during the 1st week of life; this inability to respond immunologically has been attributed to lack of functional macrophages and T cells. To determine whether B cells of newborn mice are functionally mature and therefore capable of producing antibodies to thymus (T) independent antigens, the response of 1-9-day-old C3H/HeJ mice injected with a thymus-independent polypeptide, poly(DTyr,DGlu)-polyDPro- -polyDLys was compared to that of their littermates injected with a thymus-dependent immunogen, poly(LTyr,LGlu)-polyLPro- -polyLLys. No antibodies were detected in 1- or 2-day-old mice immunized with the T-dependent antigen, as revealed by haemagglutination and haemolytic plaque-forming cell assays, performed 6 days after injection of the antigen. Injection of 3-day-old animals with the thymus-dependent immunogen resulted in significant immune responses which increased with age. In contrast, 1- and 2-day-old mice responded to the T-independent immunogen with high antibody levels, however, in 3-day-old injected mice, the levels were lower. When 3-day-old nude mice were injected with this antigen, no decrease in the immune response was observed. Thus, newborn mice respond immunologically to a thymus-independent antigen injected at the first 2 days after birth and the antibody levels decrease with maturation of the thymus.

Age Factors↗
PubMed1975

The purification, composition, and specificity of the anti-T lectin from peanut (Arachis hypogaea).

Peanut agglutinin was purified by affinity chromatography on Sepharose-epsilon-aminocaproyl-beta-D-galactopyranosylamine. The purified lectin obtained in a yield of 150 mg/100 g of defatted peanut was homogeneous on polyacrylamide gel electrophoresis, ultracentrifugation, and gel filtration. This intrinsic sedimentation coefficient (So20,w) and the intrinsic diffusion coefficient (Do20,w) were estimated at pH 7.4 as 5.7 +/- 0.1 S and 5.0 X 10(-7) cm2s(-1), respectively. The molecular weight of the agglutinin, determined by sedimentation and diffusion and by gel filtration, was found to be 110,000. Disc gel electrophoresis and gel filtration, both in the presence of sodium dodecyl sulfate, gave a single component of Mr = 27,500 suggesting that the lectin is a tetramer composed of four subunits. Four alanine residues per 110,000 g were found by NH2-terminal analysis and the sequence of the five NH2-terminal amino acids was: ALa-Glu-Ser-Val-Thr. Each cycle in a sequenator gave a single amino acid, suggesting that the four subunits are identical. Peanut agglutinin does not contain covalently bound sugar; it is devoid of cysteine and cystine, low in methionine, histidine, and tryptophan, but rich in acidic and hydroxyamino acids. The lectin agglutinated erthrocytes of human ABO blood types equally well, but only after they have been treated with neuraminidase. Of the monosaccharides tested for inhibition of hemagglutination only D-galactose and alpha- and beta-D-galactosides were active. High inhibitory activity was found with the Discaccharide DGalbeta(1 in equilibrium 3)DGalNAc and with the disialylated glycoproteins: alpha1-acid glycoprotein, fetuin, glycophorin, and human blood group NN or MM antigen. These desialylated glycoproteins also reacted with the lectin to form precipitin bands in Ouchterlony double diffusion in agar.

Amino Acid Sequence↗
PubMed1975

A micro-method for quantitative determination of acylneuraminic acids from erythrocyte membranes.

A micro-method is presented which enables the fast and exact determination of acid-hydrolyzed acylneuraminic acids in erythrocyte membranes. Erythrocytes from 1 ml of human and rabbit blood containing ACD buffer are, washed and hemolyzed on Millipore filters of pore size 1.2 mu. Acylneuraminic acids are released from the erythrocyte membranes still on the filters under the optimal conditions of 0.1 N HCl at 80 degrees C for 50 min. A prerequisite for the determination of the true amount of acylneuraminic acids using the periodic acid/thiobarbituric acid assay is the small-scale extraction of lipids from the hydrolysate and anion-exchange chromatography of acylneuraminic acids. The values thus obtained must be corrected, as 20% of acylneuraminic acids are destroyed during acid hydrolysis. In samples of human blood from 10 healthy individuals, on an average 223 nmol acylneuraminic acids per ml of packed erythrocytes were found, and in the same amount of rabbit erythrocytes, 1e method for a screening of the acylneuraminic acid content of erythrocyte membranes in hemolytic diseases or of other cell membranes is discussed.

Animals↗