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PubMed1982

Involvement of dolichol phosphates as intermediates in the mannosyl and galactosyl transferases of rat testicular germ cell Golgi apparatus membranes.

Isolated Golgi apparatus membranes from the germinal elements (spermatocytes and early spermatids) of rat testis were examined for their ability to incorporate [14C]mannose and [14C]galactose into glycolipid and glycoprotein fractions. Transfer of mannose from GDP-[14C]mannose into a Lipid I fractions (GPD:MPP mannosyl transferase activity), identified as mannosyl phosphoryl dolichol, showed optimal activity at 1.5 mM manganese and at pH 7.5. Low concentrations of Triton X-100 (0.1%) stimulated transferase activity in the presence of exogenous dolichol phosphate (Dol-P); however, inhibition occurred at Triton X-100 concentrations greater than 0.1%. Maximal activity of this GDP:MPP mannosyl transferase occurred at 25 microM Dol-P. Activity using endogenous acceptor was 2.34 pmole/min/mg, whereas in the presence of 25 microM Dol-P the specific activity was 284 pmole/min/mg, a stimulation of 125-fold. Incorporation of mannose into a Lipid II (oligosaccharide pyrophosphoryl dolichol) and a glycoprotein fraction was also examined. In the absence of exogenous Dol-P, rapid incorporation into Lipid I occurred with a subsequent rise in Lipid II and glycoprotein fractions suggesting precursor-product relationships. Addition of exogenous Dol-P to galactosyl transferase assays showed only a minor stimulation, less than twofold, in all fractions. Over the concentration range of 9.4 to 62.5 micrograms/ml Dol-P, only 1% of radioactive product accumulated in the combined lipid fractions. These observations suggest that the mannose transfer involves Dol-P intermediates and also that spermatocyte Golgi membranes may be involved in formation of the oligosaccharide core as well as in terminal glycosylations.

Animals↗
PubMed1992

Purification and Characterization of Wheat beta(2-->1) Fructan:Fructan Fructosyl Transferase Activity.

Fructans are the major storage carbohydrate in vegetative tissues of wheat (Triticum aestivum L.). Fructan:fructan fructosyl transferase (FFT) catalyzes fructosyl transfer between fructan molecules to elongate the fructan chain. The objective of this research was to isolate this activity in wheat. Wheat (cv Caldwell) plants grown at 25 degrees C for 3 weeks were transferred to 10 degrees C to induce fructan synthesis. From the leaf blades kept at 10 degrees C for 4 days, fructosyl transferase activity was purified using salt precipitation and a series of chromatographic procedures including size exclusion, anion-exchange, and affinity chromatography. The transferase activity was free from invertase and other fructan-metabolizing activities. Fructosyl transferase had a broad pH spectrum with a peak activity at 6.5. The temperature optimum was 30 degrees C. The activity was specific for fructosyl transfer from beta(2-->1)-linked 1-kestose or fructan to sucrose and beta(2-->1) fructosyl transfer to other fructans (1-FFT). Fructosyl transfer from oligofructans to sucrose was most efficient when 1-kestose was used as donor molecule and declined as the degree of polymerization of the donor increased from 3 to 5. 1-FFT catalyzed the in vitro synthesis of inulin tetra- and penta-saccharides from 1-kestose; however, formation of the tetrasaccharide was greatly reduced at high sucrose concentration. 6-Kestose could not act as donor molecule, but could accept a fructosyl moiety from 1-kestose to produce bifurcose and a tetrasaccharide having a beta(2-->1) fructose attached to the terminal fructose of 6-kestose. The role of this FFT activity in the synthesis of fructan in wheat is discussed.

Journal Article↗
PubMed1979

Intracellular Localization of GDP-Fucose: Polysaccharide Fucosyl Transferase in Corn Roots (Zea mays L.).

The intracellular site of synthesis of the fucose-rich polysaccharide slime secreted by corn roots was localized by monitoring the distribution of GDP-fucose:polysaccharide fucosyl transferase activity in subcellular fractions of corn roots. Root tip sections were chopped in the presence of 0.56 molar sucrose and 100 millimolar Tris (pH 7.0). After a brief centrifugation, the homogenate was applied to a Sepharose 4B column (1.5 x 30 cm). The turbid, particulate portion of the supernatant fraction eluted at the void volume. Ninety per cent of the enzyme activity was found in the pooled particulate fractions. The particulate fraction was purified on linear sucrose gradients. Gradient fractions were characterized by buoyant density, 280 nanometer absorbance, electron microscope observation, and distributions of NADH-cytochrome c oxidoreductase and fucosyl transferase activities.TWO PEAKS OF FUCOSYL TRANSFERASE ACTIVITY WERE OBSERVED: one in fractions rich in smooth endoplasmic reticulum, and another in fractions rich in dictyosome cisternae and dictyosome vesicles. The data suggest that the synthesis of corn root slime begins in the endoplasmic reticulum and is completed in the dictyosomes prior to secretion; however, the possibility that more than one fucosyl transferase exists in corn roots is discusses.

Journal Article↗
PubMed1986

Purification and Properties of UDP-GlcNAc:Dolichyl-Pyrophosphoryl-GlcNAc GlcNAc Transferase from Mung Bean Seedling.

The N-acetylglucosamine (GlcNAc) transferase that catalyzes the formation of dolichyl-pyrophosphoryl-GlcNAc-GlcNAc from UDP-GlcNAc and dolichyl-pyrophosphoryl-GlcNAc was solubilized from the microsomal enzyme fraction of mung beans with 1.5% Triton X-100, and was purified 140-fold on columns of DE-52 and hydroxylapatite. The partially purified enzyme preparation was quite stable when stored in 20% glycerol and 0.5 millimolar dithiothreitol, and was free of GlcNAc-1-P transferase and mannosyl transferases. The GlcNAc transferase had a sharp pH optimum of 7.4 to 7.6 and the K(m) for dolichyl-pyrophosphoryl-GlcNAc was 2.2 micromolar and that for UDP-GlcNAc, 0.25 micromolar. The enzyme showed a strong requirement for the detergent Triton X-100 and was stimulated somewhat by the divalent cation Mg(2+). Uridine nucleotides, especially UDP and UDP-glucose inhibited the enzyme as did the antibiotic, diumycin. However, a variety of other antibiotics including tunicamycin were without effect. The product of the reaction was characterized as dolichyl-pyrophosphoryl-GlcNAc-GlcNAc.

Journal Article↗
PubMed2005

The TIP GROWTH DEFECTIVE1 S-acyl transferase regulates plant cell growth in Arabidopsis.

TIP GROWTH DEFECTIVE1 (TIP1) of Arabidopsis thaliana affects cell growth throughout the plant and has a particularly strong effect on root hair growth. We have identified TIP1 by map-based cloning and complementation of the mutant phenotype. TIP1 encodes an ankyrin repeat protein with a DHHC Cys-rich domain that is expressed in roots, leaves, inflorescence stems, and floral tissue. Two homologues of TIP1 in yeast (Saccharomyces cerevisiae) and human (Homo sapiens) have been shown to have S-acyl transferase (also known as palmitoyl transferase) activity. S-acylation is a reversible hydrophobic protein modification that offers swift, flexible control of protein hydrophobicity and affects protein association with membranes, signal transduction, and vesicle trafficking within cells. We show that TIP1 binds the acyl group palmitate, that it can rescue the morphological, temperature sensitivity, and yeast casein kinase2 localization defects of the yeast S-acyl transferase mutant akr1Delta, and that inhibition of acylation in wild-type Arabidopsis roots reproduces the Tip1- mutant phenotype. Our results demonstrate that S-acylation is essential for normal plant cell growth and identify a plant S-acyl transferase, an essential research tool if we are to understand how this important, reversible lipid modification operates in plant cells.

Acyltransferases↗
PubMed1992

Histamine N-methyl transferase: inhibition by drugs.

1. Histamine N-methyl transferase activity was measured in samples of human liver, brain, kidney, lung and intestinal mucosa. The mean (+/- s.d.) rate (nmol min-1 mg-1 protein) of histamine N-methylation was 1.78 +/- 0.59 (liver, n = 60), 1.15 +/- 0.38 (renal cortex, n = 8), 0.79 +/- 0.14 (renal medulla, n = 8), 0.35 +/- 0.08 (lung, n = 20), 0.47 +/- 0.18 (human intestine, n = 30) and 0.29 +/- 0.14 (brain, n = 13). 2. Inhibition of histamine N-methyl transferase by 15 drugs was investigated in human liver. The IC50 for the various drugs ranged over three orders of magnitude; chloroquine was the most potent inhibitor. 3. The average IC50 values for chloroquine were 12.6, 22.0, 19.0, 21.6 microM in liver, renal cortex, brain and colon, respectively. These values are lower than the Michaelis-Menten constant for histamine N-methyltransferase in liver (43.8 microM) and kidney (45.5 microM). Chloroquine carried a mixed non-competitive inhibition of hepatic histamine N-methyl transferase. Some side-effects of chloroquine may be explained by inhibition of histamine N-methyl transferase.

Adult↗
PubMed1975

Malonyl and palmityl transferase-less mutants of the yeast fatty-acid-synthetase complex.

146 independently isolated mutants of the fatty acid synthetase gene locus fas 1 were subdivided into six different complementation groups. Three of these groups, Va, Vb and Vd, have not been described before. The mutant fatty acid synthetases isolated from representatives of complementation group Vb were specifically deficient in two component enzymes at the same time, the malonyl and palmityl transferases. Among more than 180 fas 1 and fas 2 mutants systematically screened for malonyl and palmityl transferase activities no mutant was found affected in only one of these two fatty acid synthetase component enzymes. From this it is concluded that both transfer reactions are catalyzed by the same enzyme. In any malonyl transferase-less fatty acid synthetase, neither of the two known malonyl binding sites, i.e. enzyme-bound pantetheine and the non-thiol binding site, accepts malonate. This indicates that malonate is transferred to both groups by the same enzyme. So far, no acetyl transferase-less fas mutants have been characterized. On the other hand, the mutants of two fas 1 complementation groups, Va and Vd, though negative in overall fatty acid synthetase activity had no deficiency in any of the known component enzymes which can be tested in vitro. A possible interrelationship between both findings is discussed.

Acyltransferases↗
PubMed1987

Biosynthesis of Lewis fucolipid antigens in human colorectal carcinoma cells. Partial characterization of LcOse4Cer and H-1 fucolipid fucosyl transferase acceptor activities.

Purified glycolipids were tested for their ability to serve as acceptors of [14C]fucose from GDP-[14C]fucose as catalyzed by cell-free extracts and purified membrane fractions of human colorectal carcinoma cells, SW1116, cultured in serum-free medium. Purified lactotetraosyl ceramide (Gal beta 1----3GlcNAc beta 1----3Gal beta 1----4Glc-Cer or LcOse4Cer) and H-1 glycolipid (Fuc alpha 1----2Gal beta 1----3GlcNAc beta 1----3Gal beta 1----4Glc-Cer or IV2 Fuc alpha LcOse4Cer) stimulated incorporation of radioactivity into lipid-soluble glycolipid at a rate greater than ten times that of Lea glycolipid [Gal beta 1----3(Fuc alpha 1----4)GlcNAc beta 1----3Gal beta 1----4Glc-Cer or III4 Fuc alpha LcOse4Cer]. The enzymatic activities in crude and purified membrane fractions were optimized for substrate concentrations (glycolipid and GDP-fucose), detergent requirement (taurocholate), pH, time and protein. The radioactive product of H-1 fucosylation migrated as discrete and distinct bands on high-performance thin-layer chromatograms (HPTLC). Evidence for their identity with Leb fucolipid described previously [Fuc alpha 1----2Gal beta 1----3(Fuc alpha 1----4)GlcNAc beta 1----3Gal beta 1----4Glc-Cer or III4IV2 (Fuc alpha) LcOse4Cer] is presented. The radioactive product of LcOse4Cer fucosylation was mainly Lea fucolipid as determined by co-migration with authentic Lea fucolipid in three HPTLC systems as native and acetylated derivatives. Our results also indicated a low level of H-1 and Leb glycolipid synthesis from LcOse4Cer. On the basis of the optima, linearity for time, and enzyme-limiting conditions, we obtained a 12-19-fold purification of the LcOse4Cer and H-1 fucosyl transferase acceptor activities in three peaks of a sucrose gradient. The peak with the highest specific activity (peak 3) was highest in density and in Na+, K+, ATPase specific activity, although NADH-cytochrome-c reductase and UDP-GalNac transferase were also present in peak 3. The apparent Km values of LcOse4Cer acceptor activity and H-1 acceptor activity in peak 3 were significantly different (p less than 0.01) by statistical tests, 2.4 microM and 0.5 microM, respectively. These apparent Km values were much lower (10(3) X) and the pH optima were lower (4.8-5.3), than the corresponding properties reported for the alpha 1----3/alpha 1----4 fucosyl transferase purified from human milk. Our results suggest a role for the non-glycosidic moieties of the acceptors and/or the tissue-specific or primitive expression of these fucosyl transferase activities.

Antigens, Neoplasm↗
PubMed1996

Synthetic phospho-oligosaccharide fragments of lipophosphoglycan as acceptors for Leishmania major alpha-D-mannosylphosphate transferase.

Protozoan parasites of the genus Leishmania synthesise lipophosphoglycans, phosphoglycans and proteophosphoglycans that contain phosphosaccharide-repeat units of [-6Gal beta 1-4Man alpha 1-P-]. In this study, a GDP-Man-dependent alpha-mannosylphosphate-transferase activity was detected in washed Leishmania major membranes using synthetic phospho-oligosaccharide fragments of lipophosphoglycan as acceptor substrates. The divalent-cation-dependent alpha-mannosylphosphate-transferase activity had an apparent K(m) for GDP-Man of about 15-20 microM and a pH optimum of 7.0. The activity showed a requirement for a non-reducing terminal beta Gal residue and for one or more phosphodiester units preceding the acceptor site. Based on these results, the activity may be defined as a GDP-Man: Gal beta 1-4Man alpha 1-P-R alpha-mannosylphosphate-transferase. This acceptor specificity is consistent with a role for the alpha-mannosylphosphate transferase in the elongation of phosphosaccharide-repeat domains of Leishmania glycoconjugates rather than in the priming of these domains. An identical or similar activity must exist in the amastigote forms of the Leishmania that produce and secrete proteophosphoglycan material and the activity therefore represents a feasible target for the development of chemotherapeutics.

Animals↗
PubMed1997

Purification, characterization and partial amino acid sequencing of hydroxycinnamoyl-CoA:tyramine N-(hydroxycinnamoyl)transferase from tobacco cell-suspension cultures.

We report the purification of hydroxycinnamoyl-CoA:tyramine N-(hydroxycinnamoyl)transferase (THT) to apparent homogeneity in 12% yield from tobacco (Nicotiana tabacum L. cv. Xanthi) cell-suspension cultures elicited with a commercial preparation of pronase. The purification procedure employs only four chromatography steps and takes advantage of the fact that the transferase binds tightly both to phenyl-Sepharose and to hydroxyapatite. The native enzyme has a pI of 5.2 and consists of two identical or very similar subunits of approximately 24 kDa. The purified enzyme can synthesise a wide range of amides due to its relatively low specificity for cinnamoyl-CoA derivatives and hydroxyphenethylamines, but its best substrates are tyramine and feruloyl-CoA. THT follows Michaelis-Menten kinetics in the presence of low concentrations of feruloyl-CoA but negative cooperativity occurs when this concentration increases above 2.5 microM, resulting in a marked decrease of the affinity for tyramine. Large deviations from Michaelis-Menten kinetics are also observed when 3-methoxytyramine is used as acyl acceptor. The activity of tobacco THT is not affected by the addition of CaCl2 or MgCl2 but its maximal velocity is increased up to twofold by addition of ethanol to the assay mixture. It is inhibited in vitro by L-tyrosine benzyl ester, which binds reversibly to the tyramine-binding site. Experiments performed using L-tyrosine benzyl ester and caffeoyl-CoA as inhibitors confirm that feruloyl-CoA is the first substrate to add to the transferase in an ordered bi-bi mechanism. Part of the amino acid sequence of the transferase, elucidated by microsequencing of tryptic peptides, is also described.

Acyltransferases↗
PubMed1975

Galactose-1-phosphate uridyl transferase in fibroblasts: isozymes in normal and variant states.

Electorphoretic properties of galactose-1-phosphate uridyl transferase in cultured skin fibroblasts of normal humans and individuals with different enzyme variants have been studied. Normal fibroblast lysates showed four activity bands, each slower moving than the erythrocyte enzyme. The transferase variants revealed different mobilities analogous to those found in erythrocytes. These findings suggest that subunits of human transferase associate variously with one another in a manner specific for each tissue and that in transferase variant states, an altered subunit results in a characteristic alteration in electrophoretic mobility which is analogous for each tissue.

Electrophoresis, Starch Gel↗
PubMed2003

Elevated expression of O-GlcNAc-modified proteins and O-GlcNAc transferase in corneas of diabetic Goto-Kakizaki rats.

PURPOSE: The hexosamine biosynthetic pathway is one of the possible mechanisms involved in diabetic keratopathy. The purpose of this study was to examine the role of O-glycoside-linked N-acetylglucosamine (O-GlcNAc) modification of proteins in the pathogenesis of diabetic keratopathy in the Goto-Kakizaki (GK) rat, which has spontaneous development of diabetes. METHODS: An anti-O-GlcNAc antibody, an anti-O-GlcNAc transferase antibody, and digoxigenin (DIG)-labeled cRNA probes were used to examine the localization of O-GlcNAc-modified proteins, O-GlcNAc transferase protein and mRNA in the corneas of diabetic GK rats and in those of nondiabetic Wistar rats. The corneas from Wistar rats were organ cultured in control medium or in medium containing 100 micro M O-(2-acetamide-2-deoxy-D-glucopyranosylidene) amino-N-phenyl-carbamate (PUGNAc), an inhibitor of O-GlcNAcase, the enzyme that removes O-GlcNAc from proteins. The morphologic changes were examined by electron microscopy. RESULTS: In normal corneas, immunoreactive O-GlcNAc and O-GlcNAc transferase were observed in the epithelial, endothelial, and stromal cells. In the diabetic corneas, their immunoreactivities in the epithelium were increased in intensity. Morphologically, the number of hemidesmosomes in the epithelial basal cells was lower than that in those cells from the nondiabetic rats. In some areas, the basement membrane had detached from the epithelial basal cells. The PUGNAc treatment of Wistar rat corneas increased the level of O-GlcNAc immunoreactivity and caused a decrease in the number of hemidesmosomes and the detachment of corneal epithelial cells from the basement membrane. CONCLUSIONS: The elevated expression of O-GlcNAc-modified proteins and O-GlcNAc transferase may play a causative role in the corneal epithelial disorders of diabetic GK rats.

Acetylglucosamine↗
PubMed1972

Succinyl-CoA: 3-ketoacid CoA-transferase deficiency. A cause for ketoacidosis in infancy.

To explain the cause of a unique form of severe and intermittent ketoacidosis in an infant who expired after 6 months of life, tissue culture fibroblasts and post mortem tissue were examined for enzyme activities that catalyze glucose and ketoacid oxidation. No measurable succinyl-CoA: 3-ketoacid CoA-transferase (CoA-transferase) activity could be detected in homogenates of the post mortem brain, muscle and kidney tissue, or in the cultured skin fibroblasts. Since seven other enzyme activities involving both glycolysis and ketone body oxidation were present in these same tissues, it was reasonable to conclude that the observed absence of CoA-transferase activity was not an artifact of homogenate preparation. It was concluded that the absence of CoA-transferase activity resulted in a loss of intracellular homeostasis leading to ketoacidosis. In addition, the absence of this enzyme appears to be a reasonable explanation for the alteration in glucose metabolism that was previously reported in fibroblasts from this patient.

Acidosis↗
PubMed1976

Effect of salicylates on histamine and L-histidine metabolism. Inhibition of imidazoleacetate phosphoribosyl transferase.

In man and other animals, urinary excretion of the histidine and histamine metabolite, imidazoleacetate, is increased and that of its conjugated metabolite, ribosylimidazoleacetate, decreased by salicylates. Imidazoleacetate has been reported to produce analgesia and narcosis. Its accumulation as a result of transferase inhibition could play a part in the therapeutic effects of salicylates. To determine the locus of salicylate action, we have investigated the effect of anti-inflammatory drugs on imidazoleacetate phosphoribosyl transferase, the enzyme that catalyzes the ATP-dependent conjugation of imidazoleacetate with phosphoribosylpyrophosphate. As little as 0.2 mM aspirin produced 50% inhibition of the rat liver transferase. In vivo, a 30% decrease in the urinary excretion of ribosylimidazoleacetate has been observed with plasma salicylate concentrations of 0.4 mM. The enzyme was also inhibited by sodium salicylate but not by salicylamide, sodium gentisate, aminopyrine, phenacetin, phenylbutazone, or indomethacin. The last four drugs have been shown previously not to alter the excretion of ribosylimidazoleacetate when administered in vivo. Since both the drug specificity and inhibitory concentrations are similar in vivo and in vitro, it seems probable that the effect of salicylates on imidazoleacetate conjugation results from inhibition of imidazoleacetate phosphoribosyl transferase.

Anti-Inflammatory Agents↗
PubMed1980

Clinical usefulness of the simultaneous localisation of the isoenzymes of alkaline phosphate and gamma-glutamyl transferase.

Simultaneous localisation of the isoenzymes of alkaline phosphatase and gamma-glutamyl transferase was carried out on 173 serum samples from patients with hepatobiliary and bone disease to determine (i) if a better discrimination of the underlying pathology could be obtained by such an approach, and (ii) if the pathology suggested by the alkaline phosphatase isoenzyme separation could help in determining the cellular location of the gamma-glutamyl transferase isoenzymes. It was found that the localisation of the gamma-glutamyl transferase isoenzymes had, with a few exceptions, little advantage over the measurement of the total activity but that some evidence concerning the cellular location of the gamma-glutamyl transferase isoenzymes could be gained by such an approach. There was support for the view that the alpha 2-migrating isoenzyme is derived from the liver parenchymal cytoplasm, but little support for the view that the alpha 1-migrating isoenzyme is predominantly the induced microsomal enzyme or that the beta-migrating isoenzyme is the result of impaired biliary secretion.

Alkaline Phosphatase↗
PubMed1991

Expression of N-acetyl transferase in a human monocytic cell-line, U937.

1. N-acetyl transferase (NAT) catalyses the acetylation of arylamine and hydrazine drugs and other xenobiotics. The activity of one isozyme (polymorphic NAT) varies amongst individuals but the other (monomorphic NAT) does not. 2. The human monocytic cell-line U937 transcribes the gene for monomorphic N-acetyl transferase. 3. Although the gene for polymorphic N-acetyl transferase is present in these cells, its expression is not detected. 4. It is concluded that U937 cells are a useful model for studying the metabolism of arylamines and hydrazines by human monomorphic N-acetyl transferase.

Acetyltransferases↗
PubMed1988

Low levels of apolipoprotein A1 are not contributors to the low lecithin-cholesterol acyl transferase activity in premature newborn infants.

Umbilical cord sera were obtained from three groups of newborn infants; group I (n = 8) and group II (n = 12) weighed less than 1500 g and between 1500 and 2500 g, respectively. Group III (n = 16) was full term and weighed more than 2500 g. Lecithin-cholesterol acyl transferase activities, determined as the rates of esterification of [3H]cholesterol, were 0.13 +/- 0.01, 0.17 +/- 0.01, and 0.26 +/- 0.01 (mean +/- SEM) nmol/h/ml for groups I, II, and III, respectively. The adult value (n = 8) was 0.96 +/- 0.01 nmol/h/ml. The respective apolipoprotein A1 (apo-A1) levels were 52 +/- 6, 59 +/- 4, and 67 +/- 4 (mean +/- SEM) mg/dl. Serum level of apo-A1 in adults was 137 +/- 6 mg/dl. Plasma high-density lipoprotein cholesterol levels increased with gestational age. However, in newborn infants, high-density lipoprotein apo-lipoprotein B, total cholesterol, and triglyceride levels, were significantly lower than in adults. These data indicate that serum levels of lecithin-cholesterol acyl transferase activity significantly (p less than 0.01) increase whereas the levels of apo-A1 do not significantly change with the gestational age. Also, in full-term newborns, lecithin-cholesterol acyl transferase activity is only 27%, whereas apo-A1 levels are 49% of adult values. Therefore, lower levels of apo-A1 do not account for the significantly lower activity of lecithin-cholesterol acyl transferase in preterm as compared to full-term newborn infants.

Apolipoproteins A↗
PubMed1979

Intrinsic ADP-ribose transferase activity versus levels of mono(adp-ribose)protein conjugates in proliferating Ehrlich ascites tumor cells.

Transition of proliferating Ehrlich ascites tumor cells (3 days after transplantation) to the non-proliferating status (8--14 days after transplantation) was associated with an increase in total mono (ADP-ribose) protein conjugates. This increase was largely confined to the NH2OH-resistant subfraction. When the amounts of mono-(ADP-ribose) conjugates from 20% trichloroacetic acid precipitates were compared with those from 5% perchloric acid precipitates, no significant differences were seen. This fact excludes histone H1 as a major mono (ADP-ribose) acceptor in vivo in these cells. Transition to the resting state was also associated with a small decrease in NAD levels, and with no significant changes of total ADP-ribose transferase activity. However intrinsic ADP-ribose transferase activity as expressed in permeabilized cells was increased, being correlated with the changes in the level of the NH2OH-resistant mono (ADP-ribose) protein conjugates. This shows that alterations in intrinsic transferase activity may, in general, indicate similar alterations in major subfractions of ADP-ribose conjugates. Intrinsic ADP-ribose transferase activity exhibited an inverse relationship to ornithine decarboxylase activity.

Adenosine Diphosphate Ribose↗