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Medical Biochemistry Commons

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Full-Text Articles in Medical Biochemistry

Patterns Of Polyadenylation Site Selection In Gene Constructs Containing Multiple Polyadenylation Signals., Roger Denome, Charles Cole Nov 1988

Patterns Of Polyadenylation Site Selection In Gene Constructs Containing Multiple Polyadenylation Signals., Roger Denome, Charles Cole

Dartmouth Scholarship

We have constructed a series of plasmids containing multiple polyadenylation signals downstream of the herpes simplex virus type 1 (HSV) thymidine kinase (tk)-coding region. The signals used were from the simian virus 40 (SV40) late gene, the HSV tk gene, and an AATAAA-containing segment of the SV40 early region. This last fragment signals polyadenylation poorly in our constructs and not at all during SV40 infection. All plasmids contained the SV40 origin of replication. Plasmids were transfected into Cos-1 cells; after 48 h, cytoplasmic RNA was isolated and the quantity and 3'-end structure of tk mRNAs was analyzed by using S1 …


Insulin Stimulates The Dephosphorylation And Activation Of Acetyl-Coa Carboxylase., Lee A. Witters, Thomas D. Watts, Diana L. Daniels, Joseph L. Evans Aug 1988

Insulin Stimulates The Dephosphorylation And Activation Of Acetyl-Coa Carboxylase., Lee A. Witters, Thomas D. Watts, Diana L. Daniels, Joseph L. Evans

Dartmouth Scholarship

The mechanism underlying the ability of insulin to acutely activate acetyl-CoA carboxylase [acetyl-CoA: carbon-dioxide ligase (ADP-forming), EC 6.4.1.2; AcCoA-Case] has been examined in Fao Reuber hepatoma cells. Insulin promotes the rapid activation of AcCoACase, as measured in cell lysates, and this stimulation persists to the same degree after isolation of AcCoACase by avidin-Sepharose chromatography. The insulin-stimulated enzyme, as compared with control enzyme, exhibits an increase in both citrate-independent and -dependent activity and a decrease in the Ka for citrate. Direct examination of the phosphorylation state of isolated 32P-labeled AcCoACase after insulin exposure reveals a marked decrease in total enzyme phosphorylation …