Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: DrugBank:APRD00369 (ROS)
 19,271 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Both the number of exposed SH-groups and the rate of reaction with 5,5'dithiobis-2-nitrobenzoic acid (DTNB) in walleye pollock and bovine rhodopsin depend on a degree of native structure of the preparation to be investigated. The preparations studied can be arranged in the order of increase of these parameters as follows: ROS less than rhodopsin extracted by digitonin less than triton X-100 less than cetyltrimethylammonium bromide (CTAB) less than sodium dodecylsulphate (SDS). After illumination of ROS and digitonin, triton X-100 and CTAB-solubilized rhodopsin, and increase was observed in the number of modified SH-groups. Dark and bleached samples of walleye pollock rhodopsin exhibited a faster rate reaction and a more number of modified SH-groups as compared to bovine preparation. The differences between bovine and walleye pollock preparation disappeared after complete opsin unfolding as a result ROS solubilization in SDS. Six SH-groups per molecule of rhodopsin were modified in both preparation under these conditions. No differences in the number of cysteine residues (10--11), disulfide groups (2), acid (35--40) and base (25--30) titratable groups per rhodopsin molecule were found between bovine and walleye pollock ROS membranes. The isoelectric point of both rhodopsin preparations was within the pH range 5.2--5.6. After proteolysis of ROS with papain, a fragment with molecular weight 24500 +/- 1000 was detected, which contained the same number of SH-groups and cysteine residues as in the case of intact rhodopsin. The results obtained suggest that, in spite of a similar primary structure, the walleye pollock visual pigment has more "loose" and "fluid" space packing in the ROS membrane than the bovine pigment.
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PMID:[Accessibility of sulfhydryl groups to 5,5'-dithiobis-2-nitrobenzoic acid and acid-base properties of bovine and walleye pollock rhodopsin preparations]. 2 81

Using topo-optical staining reactions, the presence and molecular order of three structural components of outer segments of frog retina were studied. These components included (1) an acidic polysaccharide texture, (2) free aldehyde groups which arise during formalin fixation and (3) the oligosaccharide chains of rhodopsin. Quantitative measurements of the dye binding and birefringence effects arising from the individual structural components in rod outer segments were made. Results indicated that all three structural components had a rather well-defined orientation within the ROS. The spherulites phagocytized from the apical ends of ROSs by the pigment epithelium also demonstrate preferred orientation of the three structural components investigated.
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PMID:Orientation of acidic polysaccharides and rhodopsin-oligosaccharides in frog retinal rod outer segments. 7 56

The authors studied the appearance and behavior of complement-fixing anti-ROS antibodies in the sera of GrCh rabbits following one or two intracutaneous injections of retinal antigens emulsified in Freund's complete adjuvant (KFA). Fourteen different antigenic preparations from heterologous, homologous, and autologous retinal components incorporated in KFA were tested and compared. Apart from the supernatant of a centrifuged homogenized preparation of homologous retina, all immunogens generally induced anti-ROS antibodies. The antibody titers (reciprocal values) reached a maximum 4 to 8 weeks post injection, at only low levels. The changes in antibody concentrations showed some relationship to the quality and dose of the immunogens. Anamnestic effects following reinjection reached maximum values within as little as 5 to 14 days. Animals not developing chorioretinitic lesions showed higher antibody titers more frequently than rabbits with clinically confirmed disease. Provided there is sufficient relevance of the humoral reactions observed, the complement-fixing antibodies we found in our experiments are more likely to have protective than pathogenic functions.
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PMID:[Experimental allergic chorioretinitis. Appearance and behavior of complement-fixing anti-ROS antibodies in the sera following immunization with retinal antigens (author's transl)]. 30 68

Ten clinical observations concerning six families with familial myeloproliferative disorders are reported. Family no. 1 : two brothers, RES with myelosclerosis and ROS with chronic myeloid leukemia. Family no. 2 : PG atypical myeloproliferative syndrome and his brother polycythemia vera. Family no. 3 : DF myelosclerosis and her son (DR) polycythemia vera. Family no. 4 : DM, polycythemia vera, the mother and a sister with splenomegaly. The brother died with myelofibrosis. Family no. 5 : GA and ML, cousins with polycythemia vera. Family no. 6 : MB and ZG, a brother and sister with polycythemia vera. No consanguinity and no toxic, infections or malignant etiology were found in these families. The literature reviewed emphasises the rarity of the familial incidence of myeloproliferative disorders.
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PMID:[Familial myeloproliferative syndromes. Study of 6 families and review of literature]. 35 25

Measurements of total oscillatory impedance (ROS) together with spirometric and body plethysmographic determinations were made in adults and children and the results were compared. In adults (n = 260) correlation was less close (r = 0.53) than it was in 88 children (r = 0.82). Even if ROS was of similar magnitude the phase shift between pressure and flow tended to be more negative than it was in children. These differences are presumably due to anatomical differences between the adult and the growing lung. In interpretation of the results it is suggested that the differences in the ratio: airways compliance/airways resistance reflect changes arising from age and disease processes.
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PMID:[The value of measurements of oscillatory resistance in the evaluation of lung function. A comparative study in adults and children (author's transl)]. 46 63

Kinetic parameters of photoinduced permeability increase of artificial lipid membranes, modified by ROS fragments (tau20 degrees C = 20 mesec Ea = 33 +/- 2 kcal/mole) coincides with appropriate parameters of photoinduced protein fluorescence intensity decrease and ROS fragments absorption spectra change (metarhodopsin I leads leads to metarhodopsin II transition). Hydroxylamine accelerates this process, its rate is proportional to hydroxylamine at concentrations lower than 0.6 M.
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PMID:[Molecular mechanisms of receptor. II. Identification of the conformational transition of rhodopsin responsible for the leading edge of the photoresponse of artificial lipid membranes modified by fragments of the outer segment of rods]. 61 19

Intestinal tract infection by Chlamydia psittaci was demonstrated in one cattle herd by isolation from faecal specimens, using embryonated eggs. Such infections were observed in all animals younger than 12 months, in 60% of the heifers and in none of the adult cows. The presence of infection correlated (r=0.511) with the serum titre of compliment fixation antibodies against chlamydial antigen. Young calves, which were spontaneously infected with Chlamydia postnatally, developed ileitis and moderate interstitial pneumonia. The results of histological sections and isolation of the agent from tissue specimens indicated Chlamydia to be the cause of these conditions. The strain isolated (ROS DK/KVL 6/B3) was identified as C. psittaci. The morphology of the organism and it's pathogenicity in guinea-pigs were studied. In embryonated eggs, a dose-response curve was demonstrated for the ROS strain, which differed in that respect from another member of this species tested, viz. EBA (59-795).
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PMID:Chlamydia psittaci infection in Danish cattle. 71 20

The rate of rhodopsin regeneration in decolorized rod outer segments ROS of pollock and ruff in the presence of exogenous 11Z-retinal is found to depend slightly on the temperature. The Arrhenius curve is linear within 0--20 degrees C and 0--30 degrees C in case of pollock and black ruff ROS respectively. The increase of the regeneration temperature above the upper limit results in both cases in the decrease of the chromophore binding rate due to the temperature denaturation of fish opsin. The rate of opsin regeneration in bovine ROS is temperature-dependent within 0--50 degrees C, the Arrhenius curves having a specific break with the temperature conversion at 12--13 degrees, which indicates a different 11Z-retinal binding rate with bovine opsin at low and high temperatures. Maximal rhodopsin regeneration temperature was observed within 5--10 min. for fish ROS and 1.5 hour for bovine ROS. Trimethylcyclohexene derivatives with a side chain of about 7 carbon atoms and 13Z-retinal competitively inhibited the rhodopsin regeneration in pollock and bovine ROS, while 13E-11, 12-dehydroretinal and all-E-retinal did not effect this process. Some peculiarities of the rhodopsin regeneration process in fish are discussed in connection with the molecular organization of a lipid phase of photoreceptor membrane and chromophore-binding region.
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PMID:[Some features of rhodopsin regeneration process in the presence of exogenous 11Z-retinal in teleosts]. 71 68

Disks from bovine ROS undergo a rapid shrinkage when flash illuminated with green light (Uhl, R., et al. (1977) Biochim. Biophys. Acta 469. 113-122). This can be monitored as a light scattering transient, referred to as the P signal. In this paper the P signal is studied at various temperatures and pH. The temperature dependence of the kinetics reveals that "P" consists of two sequential reaction steps. Both appear to occur within the receptor molecule rhodopsin. The actually observed event, the shrinkage of the disk, is therefore not rate limiting under the tested conditions. Both steps of "P" take place while there is only one spectroscopically detectable reaction of the rhodopsin molecule, the metarhodopsin I-metarhodopsin II transition. This implies that there are intermediates of the rhodopsin photolytic cycle which are not evident as spectroscopically separate species. The amplitude of "P", i.e., the extent of the disk shrinkage, is independent of the state of the equilibrium between the two photoproducts absorbing at 478 and 380 nm respectively and called MI and MII. A scheme is suggested in which the irreversible decay of MI (478) triggers the disk shrinkage (and maybe transduction), and in which there is an equilibrium between MII (380) and a proposed isochromic photoproduct MI' (478).
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PMID:On the light-stimulated coupling between rhodopsin and its disk membrane environment. 72 4

Rhodopsin (opsin), lipid, and fatty acids were measured in rod outer segments (ROS's) of rats maintained for at least 2 weeks in continuous darkness or in 12 hours per day cyclic light. Average rhodopsin per eye was 1.8 nmol. for the 5 ft.-c. cyclic light groups compared to 2.4 nmol. for the dark groups of the same age. The phospholipid/opsin ratio was significantly higher after cyclic light maintenance, suggesting that slow adaptive processes control the opsin density of the ROS membranes. Estimates indicate that ROS length also depends on the long-term light environment. ROS lipid and fatty acid composition were not consistently different in dark and light groups.
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PMID:The rod outer segment phospholipid/opsin ratio of rats maintained in darkness or cyclic light. 83 82


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