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At least 955 records · Page 53Linked to original sources
PubMed1986

Complementary DNA and protein sequences of ethanol-inducible rat and human cytochrome P-450s. Transcriptional and post-transcriptional regulation of the rat enzyme.

The cDNAs encoding ethanol-inducible forms of rat and human cytochrome P-450s have been isolated, sequenced, and used to study the expression of this cytochrome P-450 during development and by various inducing agents. Polyclonal antibody against ethanol-inducible cytochrome P-450 was used to screen rat and human lambda gt11 cDNA expression libraries. The longest cDNAs obtained from each library were completely sequenced, and the deduced amino acid sequence of the rat cDNA was found to correspond to P450j based on the published amino-terminal sequence. The rat and human cytochrome P-450s both contained 493 amino acids and calculated molecular masses of 56,634 and 56,916 daltons, respectively. Human P450j shared 75% nucleotide and 78% amino acid similarities to the respective orthologous rat cDNA and deduced amino acid sequences. Amino acid alignment also revealed that P450j was 48% similar to P450b and P450e, the major phenobarbital-inducible forms, and 54% similar to P450PB1 and P450f, two developmentally regulated forms. Southern blot analyses of rat and human genomic DNAs verified that only a single gene shared extensive homology with P450j. The expression of P450j was found to be developmentally regulated. No immunodetectable protein or P450j mRNA was present in newborn rats; however, rapid increases in P450j mRNA and protein occurred within 1 week after birth in both male and female rats. The levels of P450j and its mRNA thereafter remained elevated up to 12 weeks of age in both sexes. The increases in both P450j and its mRNA paralleled the change in aniline hydroxylase activity during development. Run-on transcriptional analysis confirmed that these increases were due to transcriptional activation of the P450j gene. In contrast to transcriptional activation during development, induction of P450j by various agents such as pyrazole, 4-methylpyrazole, and acetone might be due to post-transcriptional events. A 4-fold elevation in both enzymatic activity and immunodetectable P450j was not accompanied by an increase in P450j mRNA level.

Amino Acid Sequence↗
PubMed1984

[Characterization of total RNA, messenger poly(A)+ RNA and homologous complementary DNA in experimental cardiac hypertrophy].

Two biological modifications are observed during adaptation of cardiac tissue to work overload: an increase in total protein synthesis and a redistribution of myosin isoenzymes. These modifications suggest that changes in DNA transcription are involved in the early response of cardiac tissue to overload. Results are reported in this paper that show a parallel increase in total and polyadenylated RNA content and concentration in cardiac overloaded tissue in the rat. The characterization of cardiac poly (A)+ mRNA by mRNA X cDNA hybridization and the identification of specific mRNAs with recombinant plasmid cDNAs are given in this report as preliminary results.

Animals↗
PubMed1984

Structure of murine complement component C3. II. Nucleotide sequence of cloned complementary DNA coding for the alpha chain.

From the inserts of two recombinant plasmids isolated from a murine liver cDNA library, the nucleotide sequence coding for the C3 alpha chain was obtained and the corresponding amino acid sequence was derived. The alpha chain portion of the mRNA is 2979 nucleotides long, specifying a polypeptide of 993 amino acids. The molecular weight of the alpha chain, in the absence of carbohydrate, was calculated from the sequence data to be 112,933. Two possible carbohydrate attachment sites were predicted at residues 269 (Asn) and 947 (Asn). In addition, the positions for two putative factor I cleavage sites were predicted from a comparison with the cleavage sites in the human C3 alpha chain. The C3 alpha chain contains 24 cysteine residues, 10 of these clustered in the C-terminal 175 amino acids of the alpha chain. Together with the accompanying report (Lundwall, A, Wetsel, R.A., Domdey, H., Tack, B.F., and Fey, G.H. (1984) J. Biol. Chem. 259, 13851-13856), this study completes the nucleotide and amino acid structure of the murine precursor prepro-C3 molecule.

Amino Acid Sequence↗
PubMed1984

Plasmodium falciparum complementary DNA clones expressed in Escherichia coli encode many distinct antigens.

A library of cDNA clones expressing antigens of the asexual blood-stages of Plasmodium falciparum (isolate FCQ27/PNG) was constructed in the bacteriophage vector gamma gt11-Amp3. Clones expressing P. falciparum antigens (as polypeptides fused to beta-galactosidase) were selected by their reactivity in an in situ colony immunoassay with affinity-purified malaria antibodies. A detailed analysis of 78 antigen-positive clones selected from approximately 10,000 recombinant clones has shown them to correspond to many different parasite antigens. cDNA hybridization studies on this array of 78 antigen-positive clones have so far identified 18 families of sibling clones with 22 clones as yet unassigned, the majority of which may represent additional unique sequences. Only about 20% of the clones synthesized abundant amounts of the malaria antigen/beta-galactosidase fused polypeptide but each multi-member family except one was represented by at least one clone producing a fused polypeptide in abundance. Antisera have been raised against cloned malaria antigens by immunizing mice and rabbits with bacterial lysates and purified fused polypeptides, respectively. These antisera have been used to characterize the antigens in P. falciparum that correspond to the various antigen-positive clones. The variety of distinct antigens recognized by these antisera confirms that the clone library contains coding sequences for many different antigens.

Animals↗
PubMed1977

Isolation of chicken hemoglobin mRNA and synthesis of complementary DNA.

Chicken globin mRNA has been purified and partially characterized. Globin-specific sequences are found primarily as 9 S RNA, but also are found with ribosomal RNA, preferentially the 28 S moiety. The chicken globin mRNA preparation has been translated in the wheat germ and Krebs ascites cell-free systems. The products have been identified by sodium dodecyl sulfate-gel electrophoresis as the alpha- and beta-globin polypeptides. The globin mRNA is resolved into two asymmetric peaks by polyacrylamide gel electrophoresis in 98% formamide. The minor rapidly migrating peak consists primarily of alpha message while the major slowly migrating peak contains a mixture of alpha and beta messages. The synthesis of cDNA has been optimized and the products analyzed by polyacrylamide gel electrophoresis in 98% formamide. The products consist primarily of full copy transcripts that can be resolved into three discrete species.

Animals↗