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Results for “Uridine Monophosphate”

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At least 19 recordsLinked to original sources
PubMed1977

The polymorphism of red cell uridine monophosphate kinase in two samples of the Italian population.

Red cell uridine monophosphate kinase polymorphism has been studied on a total of 915 individuals from two different areas of Italy (Milan and Rome). The two groups of about the same size show very similar gene frequencies. The UMPK2 allele in the pooled sample has a frequency of 2.8% which is significantly lower than those observed in the two other Caucasian populations so far examined.

Erythrocytes↗
PubMed1978

Retention improvement by topical application of uridine monophosphate into different brain areas.

This study aimed to demonstrate the effect of uridine monophosphate (UMP) on the consolidation of a brightness-discrimination reaction after topical application of this RNA precursor into the hippocampus, the neocortex or the mesencephalic reticular formation (MRF). Thirty minutes before the rats started their training in a Y-chamber, UMP was injected into each animal through cannula implanted into the particular brain area. When injected into hippocampus or MRF UMP exerted no influence on acquisition, but after epidural UMP injection an impairment of acquisition was observed. After intrahippocampal or epidural UMP application the retention test carried out 48 hour after training showed a significant improvement in retention performance, whereas UMP injection into MRF showed no influence on retention. Consequently, the retention-improving effect of UMP is probably not induced by activation of ascending neuronal systems.

Administration, Topical↗
PubMed1978

Uridine monophosphate kinase polymorphism in two Venezuelan populations.

A study of the uridine monophosphate kinase (UMPK) electrophoretic patterns in Venezuelan individuals from the mestizo population of Caracas and from the Warao Indians of the Nabasanuka village in the Delta of the Orinoco River are reported. Among the mestizo population, the frequency of the UMPK1, UMPK2, and UMPK3 alleles was .979, .020, and .001, respectively. A higher frequency of the UMPK3 gene was seen in the highly inbred Warao Indians than any other population studied to date.

Gene Frequency↗
PubMed1976

Red cell uridine monophosphate kinase: effects of red cell aging on the activity of two UMPK gene products.

We have previously reported that uridine monophosphate kinase (UMPK) is genetically polymorphic in man, and that the UMPK2 gene product has less activity than that of UMPK1 when measured in normal red cells. In this paper we present evidence that the activity of UMPK, like that of many other enzymes, declines during red cell aging, and that the lower activity of UMPK 2, as compared with UMPK 1, is best explained by its more rapid catabolism.

Erythrocyte Aging↗
PubMed1975

Red cell uridine monophosphate kinase polymorphism in Japanese.

Samples from 635 unrelated Japanese blood doners in Tokyo were examined for their red cell uridine monophosphate kinase phenotypes using starch gel electrophoresis. Three phenotypes were found: UMPK1 (570, 89.76%), UMPK 2--1 (63, 9.92%) and UMPK 2 (2, 0.32%). The corresponding gene frequency for UMPK1 was 0.9472 and for UMPK2 was 0.0528. The UMPK2 frequency in the present study was slightly higher than the previously reported value for Caucasians in the United States, but the difference is not statistically significant. A study of 15 twin pairs and their parents was in agreement with the hypothesis of autosomal codominant inheritance for UMPK.

Erythrocytes↗
PubMed1975

Cyclization of uridine monophosphate by diethyl pyrocarbonate.

Reaction between diethyl pyrocarbonate and uridine 2'-phosphate or uridine 3'-phosphate leads to the formation in high yields of uridine 2':3'-cyclic phosphate. This reaction product was identified in experiments involving (a) ultraviolet spectrophotometry, (b) paper chromatography, (c) high voltage paper electrophoresis at both pH 3.5 and 7.4, (d) acid hydrolysis, and (e) digestion with pancreatic ribonuclease.

Alkaline Phosphatase↗
PubMed1979

Red cell uridine monophosphate kinase: a comparative study in various vertebrate species.

1. Starch gel electrophoretic patterns and activity of red cell UMP-kinase were compared in different species of vertebrates. 2. A characteristic electrophoretic pattern for each species of animal studied was found. 3. The mammals differed markedly from the rest of the vertebrate compared in having a faster electrophoretic migration. 4. Significant species differences in total UMPkinase activity could be observed.

Animals↗
PubMed1979

Initial membrane reaction in peptidoglycan synthesis. Interaction of lipid with phospho-N-acetylmuramyl-pentapeptide translocase.

The initial membrane reaction in the biosynthesis of peptidoglycan is catalyzed by phospho-N-acetylmuramyl (MurN Ac)-pentapeptide translocase (UDP-MurNAc-Ala-gamma DGlu-Lys-DAla-DAla undecaprenyl phosphate phospho-MurNAc-pentapeptide transferase). In addition to the transfer reaction, the enzyme catalyzes the exchange of [3H]uridine monophosphate with the uridine monophosphate moiety of UDP-MurN Ac-pentapeptide. Two distinct discontinuities are observed in the slopes of the Arrhenius plots of the exchange and transfer activities at 22 and 30 degrees C for the enzyme from Staphylococcus aureus Copenhagen. Anisotropy measurements of perylene fluorescence and electron spin resonance measurements of N-oxyl-4',4'-dimethyloxazolidine derivatives of 12- and 16-ketostearic acid intercalated into membranes from this organism define the lower (T1 = 16--22 degrees C) and upper (Th = 30 degrees C) boundaries of a phase transition. These values correlate with the discontinuities observed for the activity measurements. Thus, it is proposed that the physical state of the lipid micro-environment of phospho-MurNAc-penetapeptide translocase has a significant effect on the catalytic activity of this enzyme.

Cell Membrane↗
PubMedDate not supplied

[Study of acid phosphatase II from Pichia guilliermondii yeasts].

Acid phosphatase II (AP II) was isolated from the cell-free extract of Pichia guilliermondii Wickerham ATCC 9058 and partially purified. The enzyme is a non-specific phosphomonoesterase. It hydrolyzes p-nitrohenyl-phophate (NPP), beta-glycerophosphate, glucose-6-phosphate, guanosine-5'-monophosphate, adenosine-5'-monophosphate, cytidine-5'-monophosphate, uridine-5'-monophosphate, alpha-naphtylphosphate, FMN. The order of the substrates corresponds to the degree of their hydrolysis decrease. The Michaelis constant of the enzyme was 1.4-10-3 M for NPP as a substrate, pH optimum was 5.5 and temperature optimum-40C. AP II was strongly inhibited by MoO4-2, F-, inorganic phosphate, Cu2+ and Be2+. The activity of the enzyme in the yeast cells does not change noticeably during growth on media with low and high iron content.

Acid Phosphatase↗