Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Pivot Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Target Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Query: EC:3.1.26.9 (
ribonuclease
)
6,589
document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)
Column chromatographic purification and sensitivity towards enzymatic treatments of dialyzable transfer factor (TFd), the immunologically specific component of dialyzable leukocyte extract (DLE), have previously been used in its biochemical characterisation. In the present work we studied the effect of enzymes and the Sephadex G-10 chromatographic separation of the components of DLE augmenting delayed-type hypersensitivity. Skin reactivities to streptokinase-streptodornase (SK-SD) and tuberculin PPD were significantly augmented by injecting DLE into antigen-primed guinea pigs. The augmentation caused by DLE treatment correlated to the pre-existing level of immunity in the recipients. Most of the augmentory activity resided in 2 adjacent fractions, eluting early from a Sephadex G-10 column. This augmentation was destroyed by alkaline hydrolysis, by treatment with pronase, proteinase K,
ribonuclease
, and nuclease P1, but not by
alkaline phosphatase
or phosphodiesterase II. The observed sensitivities towards these enzymes, except that for
ribonuclease
, were closely similar to those described for the specific TFd component of DLE. These results are compatible with the idea that either the nonspecific augmenting and the specific TFd molecules are principally similar, or that the TFd molecules, in addition to their capacity to transfer specific immunity, also have an augmenting effect, which needs in its manifestation a sub-threshold dose of immunogen.
...
PMID:Augmentation of delayed-type hypersensitivity in antigen-primed guinea pigs by human dialyzable leukocyte extract. Chromatographic and enzymatic characterization of the active principle. 676 49
A pancreas-specific antigen was identified by immunologic techniques and purified from saline extract of human pancreas. The purified pancreas-specific antigen was shown to be homogeneous by polyacrylamide gel electrophoresis under both denaturing and non-denaturing conditions. It had a molecular weight of 44000 as estimated by gel filtration or sodium dodecyl sulfate-gel electrophoresis, and a sedimentation coefficient of 3.4 S as analyzed by sucrose gradient centrifugation. Pancreas-specific antigen possessed an isoelectric point of 4.9 and migrated to alpha-beta region upon immunoelectrophoresis. By colorimetric assay procedures, pancreas-specific antigen exhibited no enzyme activity, such as amylase, protease, esterase, lipase, acid phosphatase,
alkaline phosphatase
peroxidase, deoxyribonuclease or
ribonuclease
. Immunoreactivity of pancreas-specific antigen was sensitive to proteolytic enzymes, perchloric acid and high temperature (70 degrees C, 10 min); but insensitive to neuraminidase or beta-glucosidase. Immunohistochemical staining revealed that pancreas-specific antigen was located in acinar cells of human pancreas. In addition, a higher concentration of pancreas-specific antigen was detected in pancreatic juice than in the saline extract of pancreas. This newly identified pancreas-specific antigen, therefore, may be a useful marker protein in physiological studies of pancreas and pancreatic secretion.
...
PMID:Purification and characterization of a human pancreas-specific antigen. 678 69
Low dosages of chloramphenicol (25-50 micrograms/ml) brought about a 2-4-fold stimulation of acid phosphatase activity in 48 h-germinated cotton (Gossypium hirsutum) embryos. However, at high concentrations of chloramphenicol (100-1000 micrograms/ml), there was a progressive decline in enzyme activity. The stimulatory effect of the drug on acid phosphatase activity was relatively specific, since no significant stimulation of activities of proteinase, deoxyribonuclease,
ribonuclease
, o-diphenolase and peroxidase was observed in germinating cotton embryos. Chloramphenicol, however, did promote the activities of isocitric lyase and
alkaline phosphatase
. Sephadex G-200 chromatography of the enzyme fraction revealed high (230 000)- and low (106 000)-molecular-weight multiple forms of acid phosphatase in the chloramphenicol-treated embryos, in contrast with a single molecular form (mol.wt. 106 000) in the untreated embryos. Thus the treatment of cotton embryos with chloramphenicol induced both a qualitative and a quantitative change in the acid phosphatase activity. Chloramphenicol-stimulated acid phosphatase activity was strongly inhibited when Pi was included in the germination medium. However, the control embryos showed less pronounced inhibition of enzyme activity in presence of Pi ions.
...
PMID:Chloramphenicol stimulates acid phosphatase activity in germinating cotton (Gossypium hirsutum) embryos. 687 Aug 57
The effect of a low protein (4%) diet on the activity of the hydrolytic enzymes
ribonuclease
, deoxyribonuclease, acid and alkaline phosphatases, beta-glucuronidase and lysozyme has been studied in the spleen and thymus of weanling Wistar rats. Experimentation was carried out over 20 and 30 days, and comparisons were made with well-nourished (12% protein) controls. Body weight decreased during the terminal period in protein-deficient animals (P less than 0.001). Spleen and thymus absolute net weights also dropped significantly (P less than 0.001). In terms of organ weight relative to body weight, there was a clear decrease in thymus compared with controls (P less than 0.001). Enzyme activities expressed per total organ fell significantly. Thus, in spleen at 20 days the decrease was maximum in
ribonuclease
activity (91.15%) and minimum in acid phosphatase activity (44.09%). Thymus decreases ranged from 83.60% activity in beta-glucuronidase and 93.56% in
ribonuclease
. At 30 days decreases were accentuated; the maximum value in spleen was 92.34% lysozyme and, in thymus, 97.09% acid phosphatase. A large increase in hydrolytic activity expressed per milligram of protein was registered, especially at 30 days. This increase reached a maximum of 78.08% beta-glucuronidase in thymus and a minimum of 56.1%
alkaline phosphatase
; acid phosphatase and
ribonuclease
activities were not modified. In spleen, however, acid phosphatase (34.00%),
alkaline phosphatase
(62.50%), deoxyribonuclease (39.25%), and beta-glucuronidase (36.01%) increased, but lysozyme and
ribonuclease
enzymes decreased. We concluded that a low protein diet increases catabolism in spleen and thymus through an enhancement of lysosomal hydrolase activities.
...
PMID:Effect of protein deficiency on the lysosomal enzyme activities of the spleen and thymus of weanling rats. 731 May 38
Plasma membrane from the brush border isolated from the tegument of Hymenolepis diminuta contains membrane-bound
ribonuclease
(
RNase
) and
alkaline phosphatase
activities.
RNase
(yeast RNA substrate),
alkaline phosphatase
(p-nitrophenyl phosphate substrate), and additional membrane proteins were solubilized by sonication or treatment with the detergents dodecyl trimethylammonium bromide, beta-octyl-D-glucopyranoside, sodium dodecyl sulfate (SDS), or ZwittergentTM 3-12 (N-dodecyl-N,N-dimethyl-3-ammonio-1-propanesulfonate). At optimal conditions, greater than 90% of both enzymes and total protein were solubilized by the latter two detergents, whereas beta-octyl-D-glucopyranoside, dodecyl trimethylammonium bromide, and sonication were only partially effective. Nonionic detergents did not solubilize the membrane effectively.
...
PMID:Solubilization of membrane-bound ribonuclease (RNAse) and alkaline phosphatase from the isolated brush border of Hymenolepis diminuta (Cestoda). 739 87
Fifteen various serum and urine parameters were evaluated as indicators of renal alterations induced by lead in 82 male workers of a battery plant chronically exposed to lead (median of blood lead concentration: 2.03 mumol/l). The control group comprised 44 non-exposed healthy volunteers (0.34 mumol/l). High-molecular-mass proteins (transferrin, immunoglobulin G (IgG), (albumin)) were determined in urine as markers of glomerular integrity; low-molecular-weight proteins and parenchymal enzymes (alpha 1-microglobulin, beta 2-microglobulin, retinol-binding protein, lysozyme,
ribonuclease
, N-acetyl-beta-D-glucosaminidase (NAG), alanine aminopeptidase (AAP),
alkaline phosphatase
(AP), gamma-glutamyltransferase (GGT)) as indicators of changes in the proximal tubule; Tamm-Horsfall glycoprotein and kallikrein as markers of the distal tubule. There was a positive correlation between tubular indicators and blood lead concentration as well as the erythrocyte protoporphyrin (EPP). About 30% of the lead-exposed workers showed an increased excretion of alpha 1-microglobulin, NAG,
ribonuclease
, and/or Tamm-Horsfall protein, whereas the glomerular indicators remained unchanged. The combined determination of NAG and alpha 1-microglobulin in urine could be helpful in the early detection of lead-induced changes in the nephron.
...
PMID:Changed excretion of urinary proteins and enzymes by chronic exposure to lead. 752 73
The growth of group A human, bovine, equine and porcine rotaviruses were enhanced by pretreatment of virus with pancreatin, trypsin, protease,
alkaline phosphatase
or pepsin and incorporation of these enzymes in maintenance medium. In contrast, alpha-amylase or lipase inhibited the growth of equine and porcine rotaviruses. The other enzymes, adenosine deaminase, lactase, lysozyme,
ribonuclease
or triose-phosphate isomerase gave little or no change in the growth of all four rotaviruses.
...
PMID:Effect of enzymes on the growth of human and animal rotaviruses. 754 24
We tested the diagnostic sensitivity of various urinary analytes for detecting cadmium-induced nephropathy at an early stage. We investigated 73 healthy persons (control group 1) and individuals exposed to cadmium, either environmentally (n = 36, risk group 2) or occupationally (n = 62, exposed group 3). All data were related to limits of the central 95% reference intervals of the control group. The serum creatinine and
ribonuclease
values, indicators of the glomerular filtration rate, were not different in the three groups. In the exposed persons (group 3), proximal tubular indicators (low-M(r) proteins lysozyme,
ribonuclease
, retinol-binding protein, and alpha 1-microglobulin) were more often increased than the glomerular indices (higher-M(r) proteins transferrin, IgG, and albumin). Both the low-M(r) proteins and tubular enzymes were differently altered in their excretion rates. Alanine aminopeptidase,
alkaline phosphatase
, and N-acetyl-beta-D-glucosaminidase increased even in the risk group 2. alpha 1-Microglobulin was increased in the exposed persons whose cadmium excretion was < 5 mumol/mol creatinine. The combined determination of alpha 1-microglobulin and N-acetyl-beta-D-glucosaminidase exceeded the corresponding upper reference limits in 30% of group 2 and 39% of group 3. We recommend screening for these two analytes to detect cadmium-induced renal dysfunction at an early stage.
...
PMID:Urinary proteins and enzymes as early indicators of renal dysfunction in chronic exposure to cadmium. 848 64
For the effective application of
alkaline phosphatase
from calf intestine in Molecular Biology research highly purified enzyme and free from contaminating DNases, DNA nicking,
ribonuclease
and phosphodiesterase activities is required. We now report the use of a two-step procedure which involves chromatography on a Mimetic Blue AP-Agarose, a commercially available adsorbent and Heparin Sepharose to purify calf intestinal alkaline phosphatase from a crude commercial preparation to homogeneity. Purified enzyme preparations were free from contaminating DNases, DNA nicking,
ribonuclease
and phosphodiesterase activities and exhibited a specific activity (3.800 units/mg) which is one of the highest reported among the existing high purity commercial preparations. It is therefore concluded that the reported purification protocol can be used routinely to prepare high purity
alkaline phosphatase
suitable for use in Molecular Biology research.
...
PMID:Preparation of high purity alkaline phosphatase from calf intestine using dye-ligand chromatography. 777 49
The goal of this work was to study the effect of the most common Egyptian food items, Vicia faba beans (VF) and bran, on the carcinogenicity of dibutylnitrosamine (DBN) precursors (dibutylamine and nitrite). Mice receiving DBN precursors showed a delayed gain in body weight as well as decreased protein level and 5-nucleotidase activity. Acid
ribonuclease
,
alkaline phosphatase
, and DNA level and rate of synthesis were significantly increased compared with corresponding controls. Hepatomas and bladder papillomas developed in 60% and 40% of mice, respectively, after nine months of treatment. On the other hand, administration of VF or bran, in addition to DBN precursors, lessened the damage caused by DBN precursors alone, except DNA level and rate of synthesis were elevated. Alkaline phosphatase was also elevated when bran was administered with DBN precursors. However, these elevations were still less than corresponding elevations in mice receiving DBN precursors alone. The incidence of hepatoma was also reduced to only 20% for both groups. Meanwhile, incidence of bladder papillomas was only 20% in mice receiving VF in addition to DBN precursors, and bladder papillomas were completely absent in mice receiving bran in addition to DBN precursors. In vitro studies were also performed to clarify the effect of VF or bran on diphenylnitrosamine (DPhNA) and its formation from its precursors (diphenylamine and nitrite). The study revealed that VF and bran have the ability to eliminate nitrite and DPhNA from the reaction media and to reduce the rate of formation of DPhNA from its precursors. This reaction depends on the concentration and form of VF or bran and the duration of the reaction. Thus it is concluded that some naturally occurring food items, such as VF and bran, could protect humans against the hazardous effect of nitrosamines and their precursors.
...
PMID:Effect of Vicia faba and bran feeding on nitrosamine carcinogenesis and formation. 818 23
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