scholarly journals The presence of 5-hydroxymethylcytosine in animal deoxyribonucleic acid

1972 ◽  
Vol 126 (4) ◽  
pp. 781-790 ◽  
Author(s):  
N. W. Penn ◽  
R. Suwalski ◽  
C. O'Riley ◽  
K. Bojanowski ◽  
R. Yura
Keyword(s):  
Deoxyribonucleic Acid ◽  
Phosphorus Content ◽  
Alkaline Solutions ◽  
Small Scale ◽  
Rat Tissues ◽  
Adult Rat ◽  
Frog Brain ◽  
Rat Brain And Liver ◽  
Scale Preparation ◽  
Rat Tissue

A method is given for small-scale preparation of DNA from 1.0–1.5g of adult rat tissues. The product from brain or liver is characterized by base ratios and phosphorus content which accord with reported values for rat tissue. It is reasonably free of RNA, protein and glycogen. It contains 5-hydroxymethylcytosine at a content of about 15% of the total cytosine bases present. 5-Hydroxymethylcytosine is also demonstrable in mouse and frog brain DNA and in the crude cytidylic acid fractions obtained from RNA hydrolysates of rat brain and liver. 5-Hydroxymethylcytosine is identified by paper chromatography, u.v. spectra in acid and alkaline solutions and by its conversion into 5-hydroxymethyluracil.

A COMPARISON OF METHODS FOR THE ISOLATION OF DEOXYRIBONUCLEIC ACID FROM SMALL AMOUNTS OF RAT TISSUE

1962 ◽  
Vol 40 (1) ◽  
pp. 1167-1177
Author(s):  
C. Mezei ◽  
S. H. Zbarsky
Keyword(s):  
Amino Acids ◽  
Intestinal Mucosa ◽  
Deoxyribonucleic Acid ◽  
Phosphorus Content ◽  
Comparison Of Methods ◽  
Nitrogen And Phosphorus ◽  
Extinction Coefficients ◽  
Rat Tissue ◽  
Improved Technique ◽  
Purines And Pyrimidines

Different procedures were studied for the isolation of deoxyribonucleic acid from liver and intestinal mucosa of the rat. The DNA preparations were compared with respect to intrinsic viscosities, extinction coefficients, nitrogen and phosphorus content, and base ratios. Hydrolyzates of the DNA samples contained amino acids indicating the presence of protein or peptides in the preparations. An improved technique was developed for the elution of purines and pyrimidines from paper chromatograms.

A COMPARISON OF METHODS FOR THE ISOLATION OF DEOXYRIBONUCLEIC ACID FROM SMALL AMOUNTS OF RAT TISSUE

1962 ◽  
Vol 40 (9) ◽  
pp. 1167-1177 ◽  
Author(s):  
C. Mezei ◽  
S. H. Zbarsky
Keyword(s):  
Amino Acids ◽  
Intestinal Mucosa ◽  
Deoxyribonucleic Acid ◽  
Phosphorus Content ◽  
Comparison Of Methods ◽  
Nitrogen And Phosphorus ◽  
Extinction Coefficients ◽  
Rat Tissue ◽  
Improved Technique ◽  
Purines And Pyrimidines

Different procedures were studied for the isolation of deoxyribonucleic acid from liver and intestinal mucosa of the rat. The DNA preparations were compared with respect to intrinsic viscosities, extinction coefficients, nitrogen and phosphorus content, and base ratios. Hydrolyzates of the DNA samples contained amino acids indicating the presence of protein or peptides in the preparations. An improved technique was developed for the elution of purines and pyrimidines from paper chromatograms.

scholarly journals Rat PPARs: Quantitative Analysis in Adult Rat Tissues and Regulation in Fasting and Refeeding

Endocrinology ◽  
2001 ◽  
Vol 142 (10) ◽  
pp. 4195-4202 ◽  
Author(s):  
Pascal Escher ◽  
Olivier Braissant ◽  
Sharmila Basu-Modak ◽  
Liliane Michalik ◽  
Walter Wahli ◽  
...  
Keyword(s):  
Quantitative Analysis ◽  
Rat Tissues ◽  
Adult Rat ◽  
Fasting And Refeeding

scholarly journals Basic biochemical characterization of cytosolic enzymes in thymidine nucleotide synthesis in adult rat tissues: implications for tissue specific mitochondrial DNA depletion and deoxynucleoside-based therapy for TK2-deficiency

2020 ◽  
Vol 21 (1) ◽  
Author(s):  
Liya Wang ◽  
Ren Sun ◽  
Staffan Eriksson
Keyword(s):  
Skeletal Muscle ◽  
Mitochondrial Dna ◽  
Biochemical Characterization ◽  
Basic Knowledge ◽  
Rat Tissues ◽  
Nucleotide Synthesis ◽  
Tissue Specific ◽  
Mtdna Depletion ◽  
Adult Rat ◽  
Mitochondrial Dna Depletion

Abstract Background Deficiency in thymidine kinase 2 (TK2) or p53 inducible ribonucleotide reductase small subunit (p53R2) is associated with tissue specific mitochondrial DNA (mtDNA) depletion. To understand the mechanisms of the tissue specific mtDNA depletion we systematically studied key enzymes in dTMP synthesis in mitochondrial and cytosolic extracts prepared from adult rat tissues. Results In addition to mitochondrial TK2 a cytosolic isoform of TK2 was characterized, which showed similar substrate specificity to the mitochondrial TK2. Total TK activity was highest in spleen and lowest in skeletal muscle. Thymidylate synthase (TS) was detected in cytosols and its activity was high in spleen but low in other tissues. TS protein levels were high in heart, brain and skeletal muscle, which deviated from TS activity levels. The p53R2 proteins were at similar levels in all tissues except liver where it was ~ 6-fold lower. Our results strongly indicate that mitochondria in most tissues are capable of producing enough dTTP for mtDNA replication via mitochondrial TK2, but skeletal muscle mitochondria do not and are most likely dependent on both the salvage and de novo synthesis pathways. Conclusion These results provide important information concerning mechanisms for the tissue dependent variation of dTTP synthesis and explained why deficiency in TK2 or p53R2 leads to skeletal muscle dysfunctions. Furthermore, the presence of a putative cytosolic TK2-like enzyme may provide basic knowledge for the understanding of deoxynucleoside-based therapy for mitochondrial disorders.

scholarly journals Basement membrane chondroitin sulfate proteoglycans: localization in adult rat tissues.

1990 ◽  
Vol 38 (10) ◽  
pp. 1479-1486 ◽  
Author(s):  
K J McCarthy ◽  
J R Couchman
Keyword(s):  
Chondroitin Sulfate ◽  
Dermatan Sulfate ◽  
Core Protein ◽  
Rat Kidney ◽  
Basement Membranes ◽  
Rat Tissues ◽  
Adult Rat ◽  
Unique Distribution ◽  
Reichert's Membrane

Heparan sulfate proteoglycans have been described as the major proteoglycan component of basement membranes. However, previous investigators have also provided evidence for the presence of chondroitin sulfate glycosaminoglycan in these structures. Recently we described the production and characterization of core protein-specific monoclonal antibodies (MAb) against a chondroitin sulfate proteoglycan (CSPG) present in Reichert's membrane, a transient extra-embryonic structure of rodents. This CSPG was also demonstrated to be present in adult rat kidney. We report here the tissue distribution of epitopes recognized by these MAb. The ubiquitous presence of these epitopes in the basement membranes of nearly all adult rat tissues demonstrates that at least one CSPG is a constituent of most basement membranes, and by virtue of its unique distribution is distinct from other chondroitin and dermatan sulfate proteoglycans previously described.

Distribution of α1-adrenoceptor subtype proteins in different tissues of neonatal and adult rats

2000 ◽  
Vol 78 (3) ◽  
pp. 237-243 ◽  
Author(s):  
Hao Shen ◽  
Krishna G Peri ◽  
Xing-Fei Deng ◽  
Sylvain Chemtob ◽  
Daya R Varma
Keyword(s):  
Vas Deferens ◽  
Polyclonal Antibodies ◽  
Receptor Subtype ◽  
Receptor Subtypes ◽  
Rat Tissues ◽  
Adult Rats ◽  
Adult Rat ◽  
Old Rats ◽  
Kidney Liver ◽  
The Brain

Distribution of α1-adrenoceptor (α1AR) subtype (α1A, α1B, α1D) proteins in brain, heart, kidney, and liver of 1-week-old rats and in brain, heart, aorta, kidney, liver, vas deferens, prostate, and adrenal glands of adult rats was investigated by Western analysis, using receptor subtype specific polyclonal antibodies. High levels of immunoreactive α1AAR and α1DAR in brain and heart and of α1BAR in liver and heart of neonatal rats were detected. In adult rat tissues, the abundance of α1AAR protein was most marked in the brain, intermediate in heart, aorta, liver, vas deferens, and adrenals, and minimal in the kidney and prostate; relative to other tissues, the expression of α1BAR was higher in brain and heart and that of α1DAR in brain. All the three receptor subtypes increased with age in the brain cortex, whereas the abundance of α1BAR increased in the heart but decreased in the liver; α1AAR and α1DAR in liver, kidney, and heart were not affected by age. It is concluded that α1AR subtypes are widely expressed in different neonatal and adult rat tissues.Key words: α1A-adrenoceptors, α1B-adrenoceptors, α1D-adrenoceptors, α1-adrenoceptor proteins.

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