UScholar Works
 
Filters: Department: "Oncological Sciences" Collection: "ir_uspace" Year End: 1979
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CreatorTitleDescriptionSubjectDate
1 Capecchi, Mario R.Altered enzymes in drug-resistant variants of mammalian tissue culture cells.Two selective procedures are compared in an effort to isolate variants of mouse L cells containing structural gene mutations. Among the resulting variant cloned cell lines are found two types of alterations in theenzyme hypoxanthine phosphoribosyl transferase (EC 2.4.2.8.) (1): enzyme with altered ...Drug Resistance; Azaguanine; Clone Cells; Hypoxanthines1973-11
2 Capecchi, Mario R.Characterization of three proteins involved in polypeptide chain termination.At each stage of elongation, the growing polypeptide chain is bound to the ribosome-messenger RNA complex through the transfer RNA of the most recently incorporated amino acid residue. When the chain is complete, the last polypeptide-transfer RNA (tuna) ester linkage is cleaved, releasing the chain ...Anti-Bacterial Agents; Phenylalanine; Stimulation, Chemical1969
3 Capecchi, Mario R.Initiation of E. coli proteins.Recent experiments and theoretical arguments suggest that formylmethionyl sRNA is employed as an initiator of protein synthesis. Studies also indicated that other phage proteins synthesized in the in vitro system were initiated with formylmethionine. These observations provided a basis for believin...Alanine; Chromatography, Paper; Dipeptides1966-06
4 Capecchi, Mario R.N-formylmethionyl-sRNA as the initiator of protein synthesis.A bizarre fast about Nterminal groups of bacterial proteins. Instead of a random mixture, that the great majority of N-terminal groups were either methionine or alanine. This finding suggested that methionine and alanine constituted start signals for the initiation of polypeptide chains. Alternative...Electrophoresis; Formates; In Vitro; Methionine1966-01-01
5 Capecchi, Mario R.Polypeptide chain termination in vitro: isolation of a release factor.The growing polypeptide chain remains bound to the ribosome-messenger RNA complex through the sRNA carrying the last amino acid incorporated into the polypeptide chain.' On completion of the polypeptide chain a mechanism must exist for releasing it from the protein-synthesizing machinery. To date, m...Carbon Isotopes; Phenylalanine; Proteins1967-09-01
6 Capecchi, Mario R.Polypetide chain termination. Purification of the release factors, R1 and R2, from Escherichia coli.We have extensively purified the release factors RI and Rz from Escherichia coli. These proteins can each mediate polypeptide chain termination. The physiological substrate for this reaction is a completed polypeptide chain in a peptidyl- transfer RNA-messenger RNA-ribosome complex. The reaction con...Acrylates; Detergents1971-02-25
7 Gussin, Gary N.; Capecchi, Mario R.Protein synthesis directed by DNA phage messengers.Even through the amino acids corresponding to most of the 64 nucleotide triplets are now known, several important aspects of the genetic code are not yet fully understood. In particular we need more knowledge about the "punctuation marks" of the code-for example, the signals necessary for the initia...Carbon Isotopes; Escherichia coli; Genetic Code; Methionine1967-09-01
8 Capecchi, Mario R.Purification and characterization of mouse hypoxanthine-guanine phosphoribosyltransferase.Hypoxanthine-guanine phosphoribosyltransferase (HGPR transferase) (EC 2.4.2.8) has been purified approximately 4500-fold to apparent homogeneity from mouse liver. The procedure involves the use of affinity chromatography and was designed to be readily adaptable to small scale isolations. The enzyme ...Buffers; Centrifugation, Density Gradient; Chromatography, Affinity; Chromatography, Gel; Chromatography, Ion Exchange; Electrophoresis, Polyacrylamide Gel1975-01-31
9 Capecchi, Mario R.Selective degradation of abnormal proteins in mammalian tissue culture cells.The degradation rates of several missense mutants of hypoxanthine-guanine phosphoribosyltransferase (EC 2.4.2.8) in mouse L cells are compared to those of the wild-type enzyme. Although the rates of total protein breakdown in the mutant cell lines are identical to that of the parental L cell line, ...Gene Expression Regulation; Mice, Transgenic; Microscopy, Fluorescence1974-12-01
10 Capecchi, Mario R.Yeast super-suppressors are altered tRNAs capable of translating a nonsense codon in vitro.tRNA isolated from two different yeast super-suppressor strains translates a known nonsense mutation in vitro, whereas tRNA from a closely related nonsuppressing strain does not. Suppression was assayed by translation of RNA isolated from an amber coat mutant of bacteriophage Qbeta (GB11) in a prote...Codon; Escherichia coli; Protein Biosynthesis1975-11
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