Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0040822 (tremor)
 18,428 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Propagules of Rhizoctonia solani grown in modified Czapek's medium containing sodium polypectate or carboxymethyl cellulose as a sole carbon source produced both extracellular and cell-bound polygalacturonase (PG), and cellulase (Cx), respectively. The cell-bound enzymes can be released to various extents by shaking the germinating propagules in solutions of NaCl, KCl, phosphate buffer, Na2EDTA (ethylenediaminetetraacetate), detergents such as Triton X-100 (octyl phenoxypolyethoxyethanol), Tween 80 (polyoxyethylene sorbitan monooleate), Celmusol, and distilled water. Sodium dodecyl sulfate (SDS) inactivated both PG and Cx but did no affect Cx activity in phosphate buffer solution. PG was more easily released by salts from the mycelium of R. solani than Cx. The release of both enzymes was a passive process and was not due to an osmotic effect. The amount of the cell-bound fraction was correlated with the total amount of the extracellular fraction rather than with the mycelial growth. At least one-third of the cell-bound fractions of both enzymes was found to be associated with the cell wall fraction of the mycelium.
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PMID:Release of cell-bound polygalacturonase and cellulase from mycelium of Rhizoctonia solani. 80 41

Calcium-activated neutral protease (CANP) in normal and dysmyelinating mutant, paralytic tremor (PT) rabbit myelin and premyelin fractions was studied using immature (4-5 wk) or adult animals. The enzyme was estimated by determination of its catalytic activity as well as by using immunoblot analysis after SDS-PAGE separation. The presence of two forms of CANP--one activated by calcium in the micromolar concentration (mu CANP) range and the other exhibiting low calcium sensitivity in the millimolar concentration range (m-CANP)--was found in the myelin and premyelin fractions. The developmental pattern of the enzyme activity was different for each of these two enzyme isoforms depending on the fraction studied. The higher activity on CANP (both isoforms) found in PT myelin and premyelin could be related to delayed myelination and/or to the higher turnover rate of already formed myelin. These results suggest complex and specific roles for these isoenzymes during myelin formation as is discussed further in this article. Our results confirm the extensive degradation of myelin basic protein (MBP), proteolipid protein (PLP), and, to a lesser extent, the other myelin proteins by endo- and exogenous CANP. This degradation process was significantly elevated in PT rabbit myelin. Moreover as was shown by two-dimensional gel electrophoresis, calcium-controlled proteolysis in nonmutant rabbits affected the net-charge of MBP in a manner similar to that reported for PT myelin, suggesting the possible involvement of CANP in the generation of charge isomers of MBP.
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PMID:Calcium-activated neutral protease (CANP) in normal and dysmyelinating mutant paralytic tremor rabbit myelin. 141 20

The antiviral activity of three types of spotted souslik interferons So IFN alpha, So IFN beta and So IFN gamma was studied. Fibroblasts of lungs (SL), kidneys (SK) of adult sousliks and skin fibroblasts of foetuses (SE) were equally sensitive to three types of souslik interferons. In contrast to So IFN beta and So IFN gamma, So IFN alpha, exhibited a high (100% of activity in homologous cells) cross species antiviral activity in mouse embryo fibroblasts (MEF) and a low (3% to 10% of the activity) in bovine embryo fibroblasts (BEF) and human embryo fibroblasts (HEF). The development kinetics of antiviral activity not only depended on the interferon type but also on the temperature of incubation. In comparison with So IFN gamma, So IFN alpha and So IFN beta activated earlier the maximal antiviral state. Low incubation temperature (26 degrees C) did not decrease but only delayed the antiviral activity of spotted souslik interferons. Mixed preparations of So IFN gamma with So IFN alpha or So IFN beta exhibited synergistic antiviral activity at physiological (37 degrees C) and low (26 degrees C) temperatures. The development of antiviral activity of So IFN beta as well that of Mu IFN alpha/beta was inhibited by plant lectins which reacted with the cell membrane compounds. All three types of souslik interferons were completely destroyed by trypsin and boiling at 100 degrees C for 1 min. and partially by SDS. Their sensitivity to shaking, beta-mercaptoethanol and mouse antisera against So IFN beta was different in relation to the interferon type.
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PMID:Characterization of antiviral activity of spotted souslik (Spermophilus suslicus) interferons. 244 74

A simple, rapid SDS-Page method for protein profiles analysis of Actinomyces species was developed. Eighteen strains (12 reference strains and 6 fresh isolates) representing four species were used in this study. Eight detergents were tested for protein extraction. Cell extracts were obtained by shaking the bacteria suspended in a solution containing a detergent and glass beads. After electrophoresis, according to the Laemmli's technique, two protein stain procedure were tested (Coomassie blue and silver stain). Best results were obtained with 0.5% Triton X-100 for 4 h and the silver stain procedure of Oakley. Protein profiles analysis showed that the method is reproducible and distinguishes not only species but sometimes also subspecies.
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PMID:Improved SDS-Page method for protein profiles analysis of actinomyces species. 246 59

One serotype antigen, agglutinogen 3, from Bordetella pertussis, (strain M2, serotype 1.3), has been purified. The purification procedure included acetone drying of cells harvested from shaking cultures. Agglutinogens were extracted in phosphate buffered saline. Crude extract was heat treated at 80 degrees C for 5 min and precipitated by ammonium sulphate between 25 and 60% saturation at 4 degrees C, providing 50% of the total activity and a five-fold purification. Further purification was attempted by gel filtration chromatography using a TSK-G3000 SW column. The ammonium sulphate precipitated fraction was also separated by anion exchange chromatography using a Mono Q HR 5/5 column. The purification work indicated that agglutinogen 3 is associated with several other substances and that this property can lead to purification difficulties. The isolation procedure was monitored by an agglutination-inhibition assay. The peak fraction from the ion exchange chromatography was purified up to 27-fold according to the specific activities (inhibition units per mg protein). The yield was only 1% due to severe loss of activity. In the gel filtration chromatography agglutinogen 3-activity eluted with a maximum activity corresponding to a molecular weight near 450,000. SDS-PAGE analysis indicated that agglutinogen 3 might have a subunit molecular weight of 20,800.
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PMID:Purification and preliminary characterization of agglutinogen 3 from Bordetella pertussis. 287 4

The acrosomal matrix of hamster spermatozoa was enriched and characterized. Acrosomal matrices were released from spermatozoa with shaking in a pH 5.2 buffer containing Triton X-100 and protease inhibitors, and enriched on a glass-bead column. Phase-contrast microscopy indicated that 70-80% of the acrosomal matrices were released from the spermatozoa and only minor contamination from sperm heads was detected. Transmission electron microscopy confirmed the low level of contamination in the preparation and revealed a bilaminar structure similar but not identical to that of guinea-pig acrosomal matrix. One- and two-dimensional SDS-polyacrylamide gel electrophoresis (SDS-PAGE) showed the acrosomal matrix to be a complex structure enriched for several polypeptides. Proteinase activity was demonstrated by gelatin-SDS-PAGE. The major activity corresponded to bands of relative molecular masses (Mr) of 56,000, 51,000 and 48,000 with two minor bands of Mr 30,000 and 28,000. The lectin Pisum sativum agglutinin (PSA) bound to the anterior head of spermatozoa and isolated acrosomal matrix as judged by fluorescence microscopy using FITC-PSA. Western blots of spermatozoa and acrosomal matrices followed by overlay with biotinylated PSA indicated that there are at least two PSA-binding glycoproteins of Mr 60,000 and 72,000.
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PMID:Characterization of isolated acrosomal matrices from hamster spermatozoa. 329 98

A new method for assessing antibacterial activity in amniotic fluid (AF) is presented. Sample sizes of 100 microliter were incubated at 37 degrees C in an equal amount of growth medium with inoculated bacteria. The quantification of bacterial growth was established by measuring the change in optical density with an automated spectrophotometer. In this study, Escherichia coli, type K 12, was used for inoculation and the bacterial growth was assessed after 6, 18, 30, 42, and 54 hours' incubation. The variation coefficients in intra-assay and interassay measurements were 3.8 and 5.2%, respectively. Shaking of the incubated sample significantly changed the results by increasing the number of viable cells in the most probable number method and decreasing the optical density difference in the spectrophotometric method. Nevertheless, the correlation between the results in both methods was good (r = 0.94, p less than 0.05, and r = 0.98, p less than 0.01, respectively). By filtering the AF sample before incubation, a great deal of antibacterial activity was removed. The reproducibility, simplicity, and rapidity of this spectrophotometric method of assessing antibacterial activity in AF may make it a useful clinical tool.
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PMID:Micromethod for determination of antibacterial capacity in amniotic fluid. 388 65

The extraction of fish muscle protein using SDS containing solubilization buffers was studied varying the time and the temperature of solubilization, as well as pH and SDS concentration of the buffer. At pH less than 6 the myofibrillar proteins were incompletely solubilized; temperatures of 80-100 degrees C resulted in protein degradation observable in the SDS-PAGE. Samples of fish muscle containing high amounts of formaldehyde (50 mmoles FA/kg wet weight) could only be solubilised at 100 degrees C; on the other hand it was possible to solubilize cooked and/or canned products under mild conditions (2% SDS, 1% 2-ME, pH 8.9, shaking for 2 h at 60 degrees C).
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PMID:Solubilization of fish muscle proteins with buffers containing sodium dodecyl sulfate. 401 19

Paralytic tremor (pt) is a neurological sex-linked recessive mutation in rabbits which is characterized by a coarse body tremor and limb paresis. Morphological studies showed that this mutation affects CNS myelination. Although the number of oligodendrocytes is not reduced, myelination is slower, irregular and defective. We have made a biochemical and molecular analysis of 4-wk-old mutant and normal rabbits. The amount of myelin in the mutant represents only approximately 25% of the normal level. Radioimmunoassay for myelin basic protein showed a reduction to approximately 40% in pt whole-brain homogenate but the difference was not significant in purified myelin. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis of brain homogenates followed by immunoblotting showed that all major myelin proteins are affected by the pt mutation, although to different degrees. While most of the myelin proteins are reduced to approximately 60-80% of the normal level, an important reduction to approximately 30%, was measured for the proteolipid protein (PLP). In purified myelin, the difference in PLP concentration was significant while the other specific proteins were less affected. A similar reduction in myelin-protein gene expression was detected at the mRNA level. Sex-linked transmission, low concentrations of PLP and its specific mRNA in the CNS indicate that the pt mutation primarily affects the expression of the Plp gene.
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PMID:Paralytic tremor (pt) rabbit: a sex-linked mutation affecting proteolipid protein-gene expression. 827 12

An improved method for isolation of human and Rhesus monkey band-3 separated by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) is described. Purified band-3 was obtained from human hemoglobin-free ghosts (Hb-free ghosts) after SDS-PAGE by chemical elution+sonication (CE+S). The section of the gel corresponding to the antigen was cut out, mechanically disrupted and incubated in 1% NaHCO3 containing 1% SDS, for 2 h, with shaking, at room temperature, followed by overnight incubation at 4 degrees C. The preparation was subsequently sonicated and clarified by centrifugation. Supernatants were dialyzed against distilled water, their protein contents were measured, and the presence of purified band-3 was demonstrated by SDS-PAGE. A calibration curve was developed for assay of CE+S material using densitometric evaluation of the protein profile on SDS-PAGE. An amount of 37.5 mg of Hb-free ghosts gave 3.15 mg of purified band-3 after CE+S, corresponding to an 8.4% yield. Rabbits were immunized with 50 micrograms CE+S antigen. Sera were collected and assayed by Western blot analysis against its proteolytic fragments, which were obtained from packed red blood cells by treatment with protease type VI from Streptomyces griseus (1 h at 37 degrees C), followed by extensive washing and hypotonic lysis. Specific antibodies recognized band-3 and its proteolytic fragments 60 and 63 kDa in human ghosts obtained from different blood donors, confirming the genetic polymorphism. Analogous serum obtained against the Rhesus monkey band-3 proteolytic fragment 63 kDa recognized the human antigen and its respective fragments. These results indicate the existence of similarities between these two species of band-3, suggesting the potential use of this technique in taxonomic and phylogenetic studies. Purification by CE+S is an efficient and rapid method for isolation of band-3 and its fragments with satisfactory yields and maintenance of both their immunogenic and antigenic properties.
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PMID:An improved method for the isolation of erythrocyte antigen band-3. 858 Aug 81


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