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

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Query: EC:3.1.26.9 (ribonuclease)
6,589 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The urinary enzymes alanine aminopeptidase (EC 3.4.11.2), alkaline phosphatase (EC 3.1.3.1), gamma-glutamyltransferase (EC 2.3.2.2), N-acetyl-beta-D-glucosaminidase (EC 3.2.1.30), and ribonuclease (EC 3.1.4.22) were measured in 66 healthy persons and 52 patients suffering from chronic renal diseases (pyelonephritis, glomerulonephritis). The residual renal function of patients characterized by 99mTc-diethylenetriaminopentaacetate isotope clearance was only moderately reduced. Except for gamma-glutamyltransferase, patients generally showed increased urinary enzyme excretions. N-Acetyl-beta-D-glucosaminidase was more sensitive to detect renal dysfunction than the other enzymes and the conventional parameters serum creatinine, total protein excretion, and the measurement of glomerular filtration rate. The determination of this enzyme can be recommended as a suitable diagnostic parameter in nephrology.
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PMID:Diagnostic significance of different urinary enzymes in patients suffering from chronic renal diseases. 289 Apr 51

The influence of a variety of clinical and biochemical parameters on the activities in serum of ribonuclease (RNAse) selective for polycytidylic acid (RNAse C) were examined in 90 adult patients with cancer. The clinical data base determined on each patient included: RNAse C level, carcinoembryonic antigen (CEA) level, age, sex, race, presence (or absence of metastases, type of cancer, site of metastasis, renal function blood urea nitrogen [BUN], creatinine), hepatic function (bilirubin, alkaline phosphatase), and nutritional status (percent ideal body weight, percent weight loss, and albumin). Common tumor types studied included: colon (21), lung (18), breast (15), and hepatocellular carcinoma (10). For comparison, 175 nonmalignant control patients were studied to establish the normal range for RNAse. In patients with cancer, RNAse levels were increased in 57% and CEA levels were above 10 ng/dl in 36%. Although patients with BUN greater than 25 mg/dl or creatinine greater than 1.5 mg/dl were not entered on the study, nonetheless, RNAse was significantly (P less than 0.05) associated with both BUN and creatinine. Nutritional status also had an important influence on RNAse levels as both percent weight loss and percent ideal body weight were significantly (P less than 0.05) associated with circulatory RNAse: weight loss resulted in higher RNAse levels. These results account in part for the increased RNAse levels seen in those malignant conditions such as pancreatic and lung cancer commonly associated with weight loss in advanced stage. The possibility that circulatory RNAse C determination will provide a sensitive means for assessing nutritional status in cancer patients will require prospective evaluation.
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PMID:Influence of nutritional status on circulatory ribonuclease C levels in patients with cancer. 298 Nov 45

Testosterone-treated calf thymocytes produce increased amounts of proteins, termed lipokinins, that stimulate phospholipase A2 from snake venom and mammalian tissue. The induction of these proteins by testosterone is blocked by cycloheximide and, thus, requires new protein synthesis. These proteins activate phospholipase A2 stoichiometrically. They are inactivated by boiling, trypsin or alkaline phosphatase but not by deoxyribonuclease or ribonuclease. Lipokinins significantly repair the failure of masculinization in the Tfm mouse with an X-linked deficiency of androgen-receptor. Thus, the post-receptor effects of testosterone on embryonic genitalia may be mediated through stimulation of phospholipase A2 by lipokinins. Moreover, lipokinins may be involved as stimulators of the arachidonic acid cascade, as lipocortins are inhibitors.
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PMID:John Lattimer lecture. Lipokinins: novel phospholipase A2 activators mediate testosterone effects on embryonic genitalia. 318 94

Escherichia coli strain N100 has been mutagenized by transposon mutagenesis and mutants with a cell surface leaky phenotype have been isolated. The mutant designated as E. coli N100::Tn5 excreted periplasmic proteins like ribonuclease and alkaline phosphatase. When this mutant strain was transformed with plasmids containing cloned cholera toxin genes, the toxin protein synthesized in the cells were excreted. The potentiality of this strain as a live oral vaccine for cholera has been discussed.
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PMID:Excretion of cholera toxin from Escherichia coli: a potential oral vaccine for cholera. 329 72

An inactivated gene for Bacillus amyloliquefaciens extracellular ribonuclease (barnase) has previously been cloned and sequenced following transposon mutagenesis. The intact gene could not be assembled in Escherichia coli and is presumed to be lethal. Therefore, we introduced specific mutations into the barnase gene to prevent its lethal effect. A Gln-73 mutant gene was stable in E. coli but only produced low amounts of barnase antigen. Mutants containing Asp, Gln or Arg, instead of His-102, at the active site were identified by immunological screening for barnase antigen. None of the mutant proteins with alterations at aa residue 102 possessed RNase activity. The level of barnase (Asp-102) was higher in E. coli than in B. subtilis but the protein was not processed to the correct size in E. coli. To obtain correct processing, the barnase (Asp-102) structural gene was fused to the E. coli alkaline phosphatase promoter and signal sequence (phoA). Cells containing this construct secreted correctly processed barnase (Asp-102) into the periplasmic space and culture supernatant at a level of 20 mg/l. Barnase (Asp-102) was purified and found to have an identical N-terminus and a thermal unfolding curve that was nearly identical to that of active barnase (His-102). The cloning and expression of barnase in E. coli will allow detailed analysis of barnase protein folding by molecular genetic approaches.
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PMID:Expression of Bacillus amyloliquefaciens extracellular ribonuclease (barnase) in Escherichia coli following an inactivating mutation. 329 26

Rabbit globin complementary DNA made with RNA-dependent DNA polymerase (reverse transcriptase) was used as template for in vitro synthesis of (32)P-labeled RNA. The sequences of the nucleotides in most of the fragments resulting from combined ribonuclease T(1) and alkaline phosphatase digestion have been determined. Several fragments were long enough to fit uniquely with the alpha or beta globin amino-acid sequences. These data demonstrate that the cDNA was copied from globin mRNA and contained no detectable contaminants.
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PMID:Nucleotide sequence analysis of RNA synthesized from rabbit globin complementary DNA. 413 14

1. The action of beryllium on the following enzymes has been examined: alkaline phosphatase (Escherichia coli and kidney), acid phosphatase, phosphoprotein phosphatase, apyrase (potato), adenosine triphosphatase (liver nuclei, liver mitochondria, brain microsomes), glucose 6-phosphatase, polysaccharide phosphorylases a and b, phosphoglucomutase, hexokinase, phosphoglyceromutase, ribonuclease, A-esterase (rabbit serum), cholinesterase (horse serum), chymotrypsin. Alkaline phosphatase and phosphoglucomutase are inhibited by 1mum-beryllium sulphate whereas the other enzymes are largely unaffected by 1mm-beryllium sulphate. 2. Possible mechanisms for the inhibition of phosphoglucomutase and alkaline phosphatase are discussed.
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PMID:The inhibition of enzymes by beryllium. 428 87

A pool of alkaline phosphatase subunits has been found in cells of Escherichia coli which are actively synthesizing the enzyme. The radioactive subunits from pulse-labeled cells were specifically recognized by their capacity to produce, upon incubation with Zn(++) and nonradioactive monomers, radioactive dimers with the characteristics of alkaline phosphatase. The pool of subunits was larger (10 times or more) than the amount expected to be bound to ribosomes and was bound to a rapidly sedimentable fraction from which 60% was released by ribonuclease. In a culture pulse-labeled for one-third (8 sec) of the enzyme synthetic time, the pool of radioactive monomers was 81% of the radioactive enzyme and was totally (98%) in the endoplasm. The size of the pool was increased by decreasing the dimerization rate without affecting protein synthesis. This was achieved by decreasing Zn(++) in the growth medium. It was found that the cells contained a full complement of monomers, although the level of active enzyme was low. A process subsequent to the release of the monomers from the ribosomes was found to be limiting the formation of the finished enzyme. This process affects the level of the pool of monomers independently from their synthesis.
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PMID:Alkaline phosphatase subunits and their dimerization in vivo. 487 56

Four proteins, which have been designated A, B, C and D, have been purified from human parotid saliva. These proteins are the major constituents of parotid saliva which migrate rapidly to the anode in polyacrylamide electrophoresis at pH9.5. Gel filtration and polyacrylamide electrophoresis were employed in the purification procedures. After purification all four preparations were tested for homogeneity by electrophoresis at pH2.8 and 9.5, by isoelectric focusing in the pH range 3-10, by immunodiffusion, and by sedimentation in the analytical ultracentrifuge. None of the proteins showed significant activity in assays for amylase, acid and alkaline phosphatase, protease, lysozyme, ribonuclease, peroxidase, beta-glucuronidase, beta-galactosidase, iron-binding activity and esterase. No cross-reactions were detected with antisera specific for lactoferrin and 15 serum proteins. All four proteins were rich in glutamic acid, proline and glycine and were lacking completely the sulphur-containing amino acids. Proteins A and C contained no threonine or tyrosine. Carbohydrate could be demonstrated only in protein A at a concentration of 4% of the total protein.
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PMID:Purification and partial characterization of four proteins from human parotid saliva. 500 93

Group H streptococci (strain Challis) which are competent for transformation release a bacteriocin into liquid medium which is bacteriocidal for another group H streptococcus (strain Wicky). The streptocin (STH(1)) is resistant to treatment with deoxyribonuclease and ribonuclease but is sensitive to trypsin, phospholipase C, and alkaline phosphatase. Such enzyme sensitivity experiments indicate that the bacteriocin may be a complex molecule (protein and lipid) containing phosphate groups essential for activity. STH(1), which is readily distinguishable from competence factor and bacteriophage activity, appears to have no role in the initiation of the competent state in strain Wicky. The presence of this factor in Challis culture supernatant fluids indicates that a reevaluation of earlier studies performed with the Challis-Wicky transformation system may be necessary.
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PMID:Bacteriocin production by transformable group H streptococci. 508 61


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