[A rare complication of anticoagulant therapy: retroperitoneal (iliopsoas) hematoma].
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Adult↗
Biomedical subjects
A Gruber
Publications and source records attributed to A Gruber.
[Activable phospholipase a2 of rat blood platelets].
Rat blood platelet lysate showed high phospholipase A2 activity and contained much less than activating factor much greater than which increased phospholipase A2 activity. The phospholipase A2 and the much less than activating factor much greater than were eluted together in the same first protein fraction obtained by chromatography on a G 100 Sephadex column washed with tris-HCl buffer (pH 7.2). This mixture of proteins can be further fractionated on a Sepharose Blue CL 6B column in 2 protein fractions. The first fraction eluted by tris-HCl buffer (pH 7.2) showed 10 percent of the initial phospholipase activity; the second fraction eluted by NaCl 1 M-tris HCl buffer (pH 7.2) which showed no phospholipase activity, contains activating factor; if both fractions are mixed the initial phospholipase activity is almost totally restored. In conclusion, in rat blood platelets, phospholipase activity originates in a great part from the association of an much less than activable phospholipase much greater than and an much less than activating factor much greater than.
Animals↗
[Activation of blood phospholipases by proteins present in crude trypsin extracts].
Blood phospholipase activity in increased by crude trypsin (Sigma). This activity is not induced by trypsin itself but by some proteins contained in the extract and isolated from trypsin by G 75 Sephadex filtration. Purified trypsin or pure trypsin (Fluka, Merck, Boehringer) do not increase phospholipase activity.
Chromatography, Gel↗
[Phospholipase A2 activity in rat platelets].
Rat blood platelets show phospholipase A2 activities twenty times higher than human platelets. The breakdown of PE at pH 7.2 is linear for 15 minutes. There is no degradation at pH less than 5; the maximal activity is in the pH range 5.5-7.5. The presence of Ca2+ increases the phospholipase activity; an excess is not inhibitory. The optimal activity is obtained with 16 microM substrate concentration. Substrate inhibition is observed when the concentration exceeds 25 microM.
Animals↗
[Analysis of saliva: a sign of ovulation (author's transl)].
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Electrolytes↗
[District physicians on their work in the integrated hospital. A contribution to the social problems in the district system].
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Czechoslovakia↗
Primary structure and evolutionary relationship between the adult alpha-globin genes and their 5'-flanking regions of Xenopus laevis and Xenopus tropicalis.
To investigate the evolution of globin genes in the genus Xenopus, we have determined the primary structure of the related adult alpha I- and alpha II-globin genes of X. laevis and of the adult alpha-globin gene of X. tropicalis, including their 5'-flanking regions. All three genes are comprised of three exons and two introns at homologous positions. The exons are highly conserved and code for 141 amino acids. By contrast, the corresponding introns vary in length and show considerable divergence. Comparison of 900 bp of the 5'-flanking region revealed that the X. tropicalis gene contains a conserved proximal 310-bp promoter sequence, comprised of the canonical TATA and CCAAT motifs at homologous positions, and five conserved elements in the same order and at similar positions as previously shown for the corresponding genes of X. laevis. We therefore conclude that these conserved upstream elements may represent regulatory sequences for cell-specific regulation of the adult Xenopus globin genes.
Animals↗
Use of two recombinant proteins of Trypanosoma cruzi in the serological diagnosis of Chagas disease.
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Animals↗
Trypanosoma cruzi defined antigens in the serological evaluation of an outbreak of acute Chagas disease in Brazil (Catolé do Rocha, Paraíba).
Immunoglobulin G and M humoral response to recombinant protein B13 and glycoconjugate LPPG Trypanosoma cruzi defined antigens was evaluated by ELISA in 18 patients in the acute phase of Chagas disease, who were contaminated on the same occasion. LPPG showed 100% positivity detecting both IgM and IgG antibodies, while positivity of 55-65% was observed for B13. An epimastigote alkaline extract (EPI) also showed high sensitivity for acute IgM (100%) and IgG (90%) antibodies. However LPPG had better discriminatory reactivity since with EPI two patients showed negative IgG, and several other sera presented OD values for IgG and IgM antibodies very close to the cutoff. Thus, it is suggested that detection of IgM antibodies by LPPG may be used for diagnosis of the acute phase of Chagas disease. An intense decline of IgG and IgM antibodies to the three antigens was observed in response to anti-T. cruzi chemotherapy in all acute phase patients. After treatment, six (30%) individuals maintained IgG positivity to EPI, LPPG, and B13 with lower reactivity than that measured at the acute phase. For comparison, serology of a group of 22 patients in the chronic phase of Chagas disease and also submitted to chemotherapy was determined. Positive IgM antibodies to EPI, LPPG and B13 were detected in only 5-9% cases. In all chronic-phase patients IgG antibodies highly reactive to the three antigens were present and no significant decrease resulted after benznidazole administration. These observations reinforce previous reports that treatment in the acute phase may reduce or eliminate the parasite.
Acute Disease↗
Effect of verapamil in vitro and in vivo on the accumulation of vincristine in leukemic cells from patients with low malignant lymphoma.
The accumulation of vincristine in leukemic cells and normal mononuclear cells and the effect of verapamil on cellular drug accumulation were studied. Leukemic cells were isolated from 10 patients with chronic lymphocytic leukemia, immunocytoma and prolymphocytic leukemia. Normal mononuclear cells were collected from 3 healthy subjects. The cells were incubated with [3H]-vincristine and cellular drug accumulation was determined. The accumulation of vincristine differed nine-fold between patients. The presence of verapamil, 6.6 microM, during the incubation, increased drug accumulation by 150-550%. The effect increased with increasing verapamil concentrations up to 12-15 microM. The increased accumulation of vincristine caused by verapamil also led to increased in vitro cytotoxicity. However, neither the cellular accumulation of vincristine nor the effect of verapamil on drug accumulation was correlated with the clinical response to vincristine-containing treatment regimens. To study the clinical effect of verapamil on leukemic cell accumulation of vincristine, 4 patients were given verapamil, 120 mg three times orally. The plasma concentrations of verapamil after 3 days of treatment were lower than those required to enhance vincristine accumulation in vitro. In addition, norverapamil could also be detected in all patients. Before and at the end of the verapamil treatment period, blood from the patients was incubated with [3H]-vincristine and the leukemic cells then isolated. Verapamil treatment had no effect on the accumulation of vincristine in leukemic cells.
Aged↗