Results 221 to 230 of about 210,210 (258)
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Deoxyuridine triphosphate nucleotidohydrolase of HeLa cells
International Journal of Biochemistry, 1980Abstract 1. 1. A kinetically pure preparation of dUTPase was prepared from HeLa cells. 2. 2. dUTPase is a 62,500 dalton pyrophosphatase. The Km of dUTPase for dUTP is 1.22 × 10−5 M± 0.19. In the presence of Mg2+ the Km is 0.47 × 10−5M. 3. 3. dUTPase is highly specific for dUTP and will not hydrolyze any naturally occurring deoxynucleoside
S, Mahagaokar, P N, Rao, A, Orengo
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The biotin requirement of HeLa cells
Journal of Cellular Physiology, 1981AbstractWe have examined the effect of alterations in the biotin content of the medium on the growth, viability, biotin content, and the activities of biotin‐dependent and biotin‐independent enzymes of the HeLa cells. The inclusion in the growth medium of avidin, which almost irreversibly binds with biotin (Kd, 10−15 M), results in an increase in ...
K, Dakshinamurti, L E, Chalifour
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Mitochondrial protein synthesis in HeLa cells
Journal of Molecular Biology, 1971Abstract A fraction of HeLa cell mitochondrial protein whose synthesis is unaffected by cycloheximide but blocked by chloramphenicol has been observed by acrylamide gel electrophoresis of protein released from mitochondrial preparations. In addition, it has been demonstrated that HeLa cells in the presence of puromycin produce formylmethionyl ...
J B, Galper, J E, Darnell
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1973
A primary role for the nucleolus in ribosome biogenesis has been well established and documented (1,2). It has been shown that the nucleolus, a well-characterized but variable nuclear morphological entity, represents the chromosomal location for the genes coding for ribosomal precursor RNA. In addition, the derivatives of this product, mature ribosomal
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A primary role for the nucleolus in ribosome biogenesis has been well established and documented (1,2). It has been shown that the nucleolus, a well-characterized but variable nuclear morphological entity, represents the chromosomal location for the genes coding for ribosomal precursor RNA. In addition, the derivatives of this product, mature ribosomal
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A cytoplasmic exoribonuclease from HeLa cells
Biochimica et Biophysica Acta (BBA) - Nucleic Acids and Protein Synthesis, 1977An exoribonuclease has been purified from the cytoplasm of HeLa cells. The enzyme produces 5'-AMP as the only product from poly(A). The degradation proceeds in a 3' to 5' direction, and a 3'-OH terminus is required. In addition to poly(A), the enzyme degrades other synthetic homopolymers as well as natural messenger, and ribosomal RNAs.
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