Subcellular Localization in the Ehrlich Ascites Cell of the Enzyme which Oxidizes Dihydroorotate to Orotate

1974 ◽  
pp. 422-434
Keyword(s):  
Subcellular Localization ◽  
Ascites Cell ◽  
Ehrlich Ascites ◽  
Ehrlich Ascites Cell

scholarly journals Phosphorylation of choline and ethanolamine in Ehrlich ascites-carcinoma cells

1967 ◽  
Vol 105 (2) ◽  
pp. 497-503 ◽  
Author(s):  
Cheng-Po Sung ◽  
R. M. Johnstone
Keyword(s):  
Potent Inhibitor ◽  
Ehrlich Ascites Carcinoma ◽  
Carcinoma Cells ◽  
Detectable Effect ◽  
Ascites Cell ◽  
Cell Extracts ◽  
Ehrlich Ascites ◽  
Ehrlich Ascites Cell ◽  
Stimulation Of

1. Ehrlich ascites-cell extracts convert choline and ethanolamine approximately equally well into their respective phosphoryl derivatives. 2. Choline is a potent inhibitor of ethanolamine phosphorylation, but ethanolamine has little effect on choline phosphorylation. 3. 2,3-Dimercaptopropanol, cysteine and Ca2+ inhibit ethanolamine phosphorylation, but have no detectable effect on choline phosphorylation. 4. Choline-phosphorylating activity in Ehrlich ascites-cell extracts is more stable during storage than ethanolamine-phosphorylating activity. 5. Choline phosphorylation is stimulated in the presence of benzoylcholine, succinylcholine, butyrylcholine and propionylcholine, whereas ethanolamine phosphorylation is inhibited. This relationship is reciprocal: the compounds causing the greatest stimulation of choline phosphorylation bring about the greatest inhibition of ethanolamine phosphorylation.

scholarly journals Murine cDNAs coding for the centrosomal antigen centrosomin A

1991 ◽  
Vol 98 (1) ◽  
pp. 37-43
Author(s):  
G. Joswig ◽  
C. Petzelt ◽  
D. Werner
Keyword(s):  
Cdna Library ◽  
Dna Sequences ◽  
Specific Antigen ◽  
Cdna Clones ◽  
Ascites Cell ◽  
Recombinant Phage ◽  
Cross Hybridization ◽  
Western Blots ◽  
Ehrlich Ascites ◽  
Ehrlich Ascites Cell

Screening of an induced Ehrlich ascites cell-derived lambda gt11 cDNA library with an antibody (GP1), immunoreacting specifically with centrosomal antigen(s) of interphase and mitotic cells of different species, released a partial cDNA clone (lambda P10A) encoding the carboxy-terminal section of a centrosome-specific antigen. This specificity of the clone lambda P10A could be verified by lacZ-directed antigen expression from Escherichia coli Y1089 lysogenized with the recombinant phage lambda P10A and subsequent production of centrosome-specific antibodies by means of the recombinant antigen. Using the lambda P10A insert as a probe, two types of cDNA clones were identified in a lambda gt10 cDNA library by plaque-hybridization. The inserts of PN1 type clones were 1.2 kb (kilobases) and those of PN5 type clones were 2.2 kb in length. The DNA sequence of a PN1 type clone revealed its full-length cDNA nature. The open reading frame of PN1 encodes a rather hydrophilic and highly charged 34.5 × 10(3) Mr polypeptide comprising short but apparently significant strings of 100% sequence identity with the major nuclear lamina polypeptides lamins A/C and lamin B. Restriction enzyme mapping of PN1 and PN5 inserts, cross-hybridization experiments and comparison of overlapping DNA sequences indicate that the 1.2 kb and 2.2 kb cDNAs code for the same 34.5 × 10(3) Mr polypeptide, termed centrosomin A. Western blots of Ehrlich ascites cell proteins show a second, larger GP1 antigen (centrosomin B) whose cDNA has not been cloned. It remains to be investigated whether centrosomin B is encoded by a second mRNA or whether it reflects an oligomeric or a postranslationally modified form of centrosomin A.

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