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phosphatase/mrzlica

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Stran 1 iz 954 rezultatov

Electrophoretic variability in the phosphatase system of the yellow-fever mosquito, Aedes aegypti.

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Alkaline and acid phosphatases in five inbred strains of the yellow-fever mosquito, Aedes aegypti, were compared by vertical polyacrylamide gel electrophoresis. 1. Polymorphic and monomorphic zones of enzyme activity were observed among both alkaline and acid phosphatases. 2. In the alkaline
BACKGROUND Determining the cause of fever of unknown origin (FUO) is often a vexing and difficult diagnostic process. In most cases, the signs and symptoms in adult FUOs suggest a malignant, infectious, or rheumatic/inflammatory etiology. The diagnosis of FUO may be narrowed if specific findings are
Acid phosphatase activity was measured in implanted murine CaNT tumors of varying volumes. There is a clear monotonically increasing relation between acid phosphatase activity and tumor volume. Also the tumors were subjected to either induced artificial hypoxia or hyperthermia (41.0 degrees C)
The African swine fever virus A238L protein inhibits calcineurin phosphatase activity and activation of NF-kappaB and p300 co-activator. An 82 amino acid domain containing residues 157 to 238 at the C-terminus of A238L was expressed in E. coli and purified. This purified A238L fragment acted as a
The African swine fever virus protein A238L inhibits activation of NFAT transcription factor by binding calcineurin and inhibiting its phosphatase activity. NFAT controls the expression of many immunomodulatory proteins. Here we describe a 14-amino-acid region of A238L that is needed and sufficient

Arylsulphatase A and acid phosphatase activities in plasma and leucocytes during LPS fever in the ox (Bos taurus).

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Intravenous injection of E. coli LPS (0.5 micrograms/kg) produced the biphasic elevation of rectal temperature (TR) in conscious oxen. The fever was accompanied by a significant increase of the arylsulphatase A (AsA) activities in plasma and in mononuclear leucocytes. In polymorphonuclear cells a

[Genetic variants of acid erythrocytic phosphatase as a risk factor of rheumatic fever].

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A study was made of the genetic variants (isoenzymes, phenotypes) of acid erythrocytic phosphatase (AcP) in 120 patients with rheumatic fever. There were 78 women and 42 men aged 16 to 57 years. The population data concerned with distribution of the AcP variants among the population of Moscow were

Evidence for an acid phosphatase in African swine fever virus.

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An acid phosphatase activity has been detected in purified preparations of African swine fever virus. Purified viral cores obtained after Nonidet-P40 and 2-mercaptoethanol treatment of the virus retained the activity as assayed with nitrophenyl phosphate as substrate at pH 5. Enzyme cytochemistry by

[Phosphatase activity in the lymph during a fever reaction].

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Activity of acid and alkaline phosphatases, as well as isoenzymes of alkaline phosphatase in the lymph of the thoracic lymphatic duct, hepatic lymph and the peripheral blood have been studied on rabbits in the dynamics of the fever reaction of different duration. The fever reaction was followed by
We prospectively determined the value of liver biopsy for microbiological diagnosis of infection in patients infected with the human immunodeficiency virus (HIV) who had unexplained fever and whose serum levels of alkaline phosphatase or gamma-glutamyl transferase were at least 1.5 times the upper
Heating the lower body of the mouse for up to 1.5 hours at temperatures above 41.0 degrees C causes an increase in splenic lysosomal acid phosphatase activity. For mouse temperatures up to 42.3 degrees C the change is probably due to enzyme activation, which reaches a maximum 1.5 hours after heating
Hyperthermia can be used as a possible adjuvant therapy in treatment of cancer patients. In this study, the direct effect of hyperthermia on osteosarcoma derived cell lines HOS85, MG-63 and SaOS-2 was investigated. Heat shock at 42 degrees C inhibited proliferation significantly in all three cell
The African swine fever virus (ASFV) DP71L protein is present in all isolates as either a short form of 70 to 72 amino acids or a long form of about 184 amino acids, and both of these share sequence similarity to the C-terminal domain of the herpes simplex virus ICP34.5 protein and cellular protein

Protein Phosphatase-1 regulates Rift Valley fever virus replication.

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Rift Valley fever virus (RVFV), genus Phlebovirus family Bunyaviridae, is an arthropod-borne virus endemic throughout sub-Saharan Africa. Recent outbreaks have resulted in cyclic epidemics with an increasing geographic footprint, devastating both livestock and human populations. Despite being
The DP71L protein of African swine fever virus (ASFV) shares sequence similarity with the herpes simplex virus ICP34.5 protein over a C-terminal domain. We showed that the catalytic subunit of protein phosphatase 1 (PP1) interacts specifically with the ASFV DP71L protein in a yeast two-hybrid
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