scholarly journals STAINING OF BASIC NUCLEOPROTEINS BY AN EXTRACT OF THE BLACK RASPBERRY

1974 ◽  
Vol 22 (10) ◽  
pp. 976-980
Author(s):  
LAWRENCE KASS

Methanolic extracts of the black raspberry (Rubrus occidentalis) were found to stain nuclei of normal human peripheral blood and bone marrow cells. Using filter paper spot tests, staining of both purified deoxyribonucleic acid and histone occurred at pH 4.1, but at pH 9.3 only histone was stained. Histone staining diminished above pH 9.3 and disappeared at pH 10.0. Using formalin-fixed cover slips of peripheral blood and bone marrow, methanol-raspberry staining at pH 9.3 demonstrated orange-brown staining nuclei. This study suggests that the anthocyanin group of naturally occurring dyes is capable of staining basic nucleoproteins at alkaline pH.

1989 ◽  
Vol 8 (1) ◽  
pp. 19-22
Author(s):  
C.D.L. Reid ◽  
A. Kirk

Ranitidine was added in various concentrations (25-1600 ng/ml) to clonal assays of haemopoietic progenitors of normal human peripheral blood or bone marrow. Although a significant reduction in colonies forming from granulocyte-macrophage progenitors (CFU-GM) was demonstrated at the lowest drug concentration, no significant growth suppression was seen at higher concentrations. There was no evidence for growth inhibition of either erythroid progenitors (BFU-E) or pluripotent progenitors (CFU-mix) at any of the drug concentrations studied. A direct toxic effect of ranitidine on normal haemopoietic progenitors thus appears an unlikely cause of cytopenias observed during treatment.


Blood ◽  
1987 ◽  
Vol 70 (2) ◽  
pp. 579-582
Author(s):  
LJ Weisberg ◽  
DT Shiu ◽  
PR Conkling ◽  
MA Shuman

Factor XIII is the fibrin-stabilizing factor that covalently cross- links fibrin monomers to form a highly organized, stable fibrin clot. The plasma form of factor XIII is a heterodimer, a2b2, consisting of two a-chains and two b-chains; the intracellular form, such as in platelets and placenta, is a dimer, a2, consisting of a-chains only. The catalytic function of factor XIII, a transglutaminase, resides in the a-chain. To address questions regarding sites of synthesis of factor XIII a-chain, an EcoRI restriction fragment from the protein- coding region of the factor XIII a-chain cDNA was used as a probe for Northern blot analysis. The cDNA probe showed hybridization with a single approximately 4.0-kilobase (kb) message in poly (A)+ mRNA prepared from normal human peripheral blood monocytes and normal human liver. The results demonstrate conclusively that factor XIII a-chains are actively synthesized in circulating monocytes and in liver. To our knowledge, these data represent the first demonstration of synthesis of any blood coagulation factor in primary uncultured and unstimulated monocytes or macrophage cells.


1977 ◽  
Author(s):  
Z. Jerushalmy ◽  
M. Patya ◽  
O. Sperling

Human blood platelets were gtudied for the presence of the pathway of de novo synthesis of purine nucleotides. 8 x 108 cells were incubated for 2.5 h at 37°C in 2 ml of Eagle’s Minimal Essential Medium containing Earle’s Balanced Salt Solution, 15% fetal calf serum and 20 μCi sodium [14C] formate (59 mCi/mmole). Platelets were found to incorporate 14C into total purines at a slow but detectable rate of 50–70 pmoles/8 x 108 cells/2.5 h. This incorporation was inhibited by approximately 80% at 10 mM azaserine and by 60% at 0.1 mM adenine. Adenine is known to affect the rate of purine synthesis de novo through the activity of phosphoribosylpyrophosphate amidotransferase, the first committed enzyme of this pathway. The results suggest the presence of the complete pathway of de novo synthesis of purine nucleotides in normal human peripheral blood platelets.


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