Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.1.27.4 (ribonuclease)
6,621 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Further studies on fever production by injection of leukocyte extracts or cell-free supernatant fluids from peritoneal exudates in rabbits are reported. Granulocytes collected from peripheral blood or from pleural exudates contain a heat-labile pyrogenic substance. The material in extracts of leukocytes and in peritoneal fluids, which causes fever, is destroyed by heating for 30 minutes at 90 degrees C. at pH 7.2 and at 70 degrees C. at pH 4.5. It is active in producing fever over a pH range of 2.0 to 10.5 and maintains potency for as long as 6 months at 4 degrees C. The fever-producing substance in leukocyte extracts is not dialyzable. Its activity is not destroyed by trypsin, chymotrypsin, or ribonuclease. No evidence of plasma activator or inhibitor was detected. Significant temperature elevation in the rabbit was effected by a quantity of leukocyte extract containing 0.76 mg. protein and 0.054 mg. polysaccharide. The febrile response produced by the material under study was compared with that of Menkin's pyrexin as well as with that of bacterial pyrogens. Several significant differences were noted. The properties of pyrexin are similar to those of bacterial pyrogens. Amidopyrine suppressed the febrile response to injection of leukocyte extracts, whereas neither amidopyrine nor cortisone influenced the appearance of pyrogenic material in induced peritoneal exudates. Peritoneal fluids collected from rabbits made leukopenic by HN(2) were found to contain a fever-promoting substance. Its character has yet to be determined. It is concluded that there is present in polymorphonuclear leukocytes of rabbits a heat-labile factor capable of producing fever in rabbits and that the leukocyte is probably not the only source of such a factor.
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PMID:Studies on the pathogenesis of fever. II. Characterization of fever-producing substances from polymorphonuclear leukocytes and from the fluid of sterile exudates. 1310 5

Attempts were made to isolate microsomes from Pisum sativum L. var. Alaska by low speed centrifugation of a postmitochondrial supernatant made 8 mm in Ca(2+). However, the addition of Ca(2+) in concentrations as low as 1 mm to the postmitochondrial supernatant resulted in extensive polysome degradation. Degradation was dependent on both Ca(2+) concentration and the duration of incubation. Resuspension of isolated polysomes in Ca(2+)-containing buffer did not result in degradation, whereas resuspension in Ca(2+)-containing postpolysomal supernatant did. Both Ca(2+) and a heat-labile factor in the supernatant were required for polysome degradation. The degradation in the homogenate with or without added Ca(2+) could be reduced by (a) dilution with larger volumes of grinding buffer, (b) increasing the concentration of tris-HCl in the grinding buffer, (c) adding diethylpyrocarbonate or ethyleneglycol-bis (2-aminoethylether) tetraacetic acid (a specific calcium chelator) prior to homogenization or immediately after the addition of Ca(2+). Endogenous Ca(2+) can increase the destruction of polysomes during their isolation in this tissue, presumably by activating a ribonuclease. Addition of Ca(2+) is not a useful technique for separating undegraded free and membrane-bound polyribosomes.
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PMID:Polyribosomes from Peas: III. Stimulation of Polysome Degradation by Exogenous and Endogenous Calcium. 1665 24