Effect of the high-molecular-weight component of the nutrient medium on growth of cultures of NK/Ly ascites tumor cells

1968 ◽  
Vol 66 (3) ◽  
pp. 1016-1018
Author(s):  
V. P. Nefedov
1965 ◽  
Vol 43 (7) ◽  
pp. 933-942
Author(s):  
C. P. Kenny ◽  
H. Lees

HeLa and ascites tumor cells could be cultured in a medium of bacteriological nutrient broth plus yeast RNA. There was no growth if the RNA was omitted from the medium. The growth-promoting property of the RNA resided in a high molecular weight (mol. wt. 1–2 × 105) fraction of the RNA and not in any small sequence of nucleotides.


1975 ◽  
Vol 23 (4) ◽  
pp. 251-270 ◽  
Author(s):  
A Penttila ◽  
E M McDowell ◽  
B F Trump

The effects of fixation with glutaraldehyde (GA), formaldehyde (FA), glutaraldehyde-formaldehyde (GA-FA), flutaraldehyde-osmium tetroxide (GA-Os04) and osmium tetroxide (OsO4) on cel volume were studied in control, p-chloromercuribenzene sulfonic acid (PCMBS)-treated and hypotonically-treated Ehrlich ascites tumor cells. Among the variables investigated were concentration of the tixative agent, osmolity of the buffer, total osmolaity of the fixation solution, osmolaltity of the postfixation buffer and the time of fixation and postfixation treatment; in addition, the effects of adding calcium and high molecular weight compounds to the fixative solution were studied. When the effects of standard fixatives on control, PCMBS- and hypotonically-treated cells were compared, marked differences were apparent in the behavior of control and injured cells. Control cells retained near prefixation volume in 3% GA and 3% GA-1% OsO4, swelled in 4% FA or 1% OsO4 and phosphate buffer (tkrp), whereas tpcmbs (310 mosM KRP)- and hypotonically-treated cells (103 mos M KRP) shrank in all aldehyde fixatives but swelled in 1% OsO4. Reducing the buffer osmolality had similar effects on control and injured cells although, there were variations in degree...


1973 ◽  
Vol 51 (4) ◽  
pp. 379-389 ◽  
Author(s):  
Gerald Krystal ◽  
Peter G. Scholefield

In the partial purification of uridine kinase (ATP:uridine 5′-phosphotransferase, EC 2.7.1.48) from Ehrlich ascites tumor cells, two active fractions were obtained by chromatography on Sepharose 6B. Their molecular weights, as determined by a gel filtration and sucrose density centrifugation, were approximately 120 000 and 30 000. The larger molecular weight species was less stable on incubation at 60° and slightly less sensitive to CTP inhibition than the lower molecular weight fraction. Both fractions were stabilized against heat inactivation by ATP and CTP.The two fractions displayed similar apparent Km values for uridine and ATP, similar specificities for substrates and inhibitors, and similar divalent cation requirements.In the partial purification of uridine kinase from mouse intestine, only the larger molecular weight fraction was obtained by chromatography on Sepharose 6B.In addition, some preliminary evidence for a monomer–polymer relationship between the two molecular weight species is presented.


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