Abstract:English Carriers 13 dred-fold to do so. This is why I believe in flies not over six and one half feet high, low alighting boards, and the alleyways in front of the houses instead of the rear, so as to be always near the birds. Fancy Breeds Cultivate the spirit of love toward them, and you will be paid for all such trouble, no ntatter how many birds you have. Two thousand can be kept tame and quiet as well as one hundred and they will work better. Other Habits-The coo of some birds is different from others. 1 d… Show more
“…This is not the first time that a heterogeneity of different creatine kinases has been found. It has been described in several reports on creatine kinases of various vertebrate species including human [28-301, rabbit [31,32] chick [33] and also trout [34,35]. As many separation techniques as studies have been carried out (starch gels, urea-starch gels, agarose gels, sodium dodecylsulphate/polyacrylamide gels and preparative isoelectric focusing) so that it is difficult to compare the different results with ours.…”
Purified, homodimeric creatine kinases from chicken were subjected to two-dimensional gel analysis under dissociating conditions. Each of the subunits M-creatine kinase and B-creatine kinase was resolved into a basic and an acidic subspecies with very similar mobilities in the sodium dodecylsulfate dimension. The M-creatine kinase subspecies were found in myogenic cells, fast muscle, slow muscle and the B-creatine kinase subspecies were present in heart, gizzard and brain. The creatine kinase subunits were identified in these tissues by a variety of methods like immunoreplicas of two-dimensional gels, immunoprecipitations, or coelectrophoresis with purified creatinc kinasc and all gave the same results. In the course of myogcnic development in vitro the subspecies were synthesized coordinately and no indication was found for a differential regulation of any of the subspecies of the creatine kinase subunits. No radioactive phosphorus was incorporated into either one of thc subspecies, hence phosphorylation could be ruled out as the source of heterogeneity. Furthermore, peptide mapping analysis of partial proteolytic digests did not reveal differences among the subspecies of the same subunit. Not only chicken but also rat creatine kinase displayed this type of heterogeneity. All subspecies were observed after translation of chicken RNA in a cell-free protein-synthesizing system. The heterogeneity probably might best be explained by the existence of multiple, but closely related genes for the creatine kinase subunits.Creatine kinase is a dimeric enzyme that plays a crucial role in the energy metabolism. It is especially characteristic of muscle tissue, but also occurs in other tissues [1,2]. The cytoplasmic nonmitochondrial enzymes are made up from two different kinds of subunits with a M , of 40000, the M-creatine kinase subunit and the B-creatine kinase subunit. MM-creatine kinase is found in appreciable amounts only in adult muscle, whereas BB-creatine kinase is more widely distributed in smooth muscle, chicken heart, brain and a variety of other tissues. During the differentiation of chicken myogenic cells in cultures as well as in embryonic muscle, an isoenzyme transition is observed from BB-creatine kinase to MM-creatine kinase, the form typical for the differentiated state. During this transition the subunits combine at random to yield homodimers and also active heterodimers MBcreatine kinase [3 -51. The subunits forming the active isoenzymes are very likely the products of at least two different genes as indicated by the differences of amino acid composition [6], the lack of immunological cross-reactivity [4,6,7] and differences in the metabolism of the corresponding mRNAs coding for thc two different subunits [S]. In addition M-creatine kinase is found in the M-line of adult skeletal myofibrils as well as in the myofibrils of cultured cells, suggesting a specific property of the MM-creatine kinase dimer whichAhhreviutions. M-creatine kinase and B-creatine kinase. subunit types of creatine kinase; MM-creati...
“…This is not the first time that a heterogeneity of different creatine kinases has been found. It has been described in several reports on creatine kinases of various vertebrate species including human [28-301, rabbit [31,32] chick [33] and also trout [34,35]. As many separation techniques as studies have been carried out (starch gels, urea-starch gels, agarose gels, sodium dodecylsulphate/polyacrylamide gels and preparative isoelectric focusing) so that it is difficult to compare the different results with ours.…”
Purified, homodimeric creatine kinases from chicken were subjected to two-dimensional gel analysis under dissociating conditions. Each of the subunits M-creatine kinase and B-creatine kinase was resolved into a basic and an acidic subspecies with very similar mobilities in the sodium dodecylsulfate dimension. The M-creatine kinase subspecies were found in myogenic cells, fast muscle, slow muscle and the B-creatine kinase subspecies were present in heart, gizzard and brain. The creatine kinase subunits were identified in these tissues by a variety of methods like immunoreplicas of two-dimensional gels, immunoprecipitations, or coelectrophoresis with purified creatinc kinasc and all gave the same results. In the course of myogcnic development in vitro the subspecies were synthesized coordinately and no indication was found for a differential regulation of any of the subspecies of the creatine kinase subunits. No radioactive phosphorus was incorporated into either one of thc subspecies, hence phosphorylation could be ruled out as the source of heterogeneity. Furthermore, peptide mapping analysis of partial proteolytic digests did not reveal differences among the subspecies of the same subunit. Not only chicken but also rat creatine kinase displayed this type of heterogeneity. All subspecies were observed after translation of chicken RNA in a cell-free protein-synthesizing system. The heterogeneity probably might best be explained by the existence of multiple, but closely related genes for the creatine kinase subunits.Creatine kinase is a dimeric enzyme that plays a crucial role in the energy metabolism. It is especially characteristic of muscle tissue, but also occurs in other tissues [1,2]. The cytoplasmic nonmitochondrial enzymes are made up from two different kinds of subunits with a M , of 40000, the M-creatine kinase subunit and the B-creatine kinase subunit. MM-creatine kinase is found in appreciable amounts only in adult muscle, whereas BB-creatine kinase is more widely distributed in smooth muscle, chicken heart, brain and a variety of other tissues. During the differentiation of chicken myogenic cells in cultures as well as in embryonic muscle, an isoenzyme transition is observed from BB-creatine kinase to MM-creatine kinase, the form typical for the differentiated state. During this transition the subunits combine at random to yield homodimers and also active heterodimers MBcreatine kinase [3 -51. The subunits forming the active isoenzymes are very likely the products of at least two different genes as indicated by the differences of amino acid composition [6], the lack of immunological cross-reactivity [4,6,7] and differences in the metabolism of the corresponding mRNAs coding for thc two different subunits [S]. In addition M-creatine kinase is found in the M-line of adult skeletal myofibrils as well as in the myofibrils of cultured cells, suggesting a specific property of the MM-creatine kinase dimer whichAhhreviutions. M-creatine kinase and B-creatine kinase. subunit types of creatine kinase; MM-creati...
“…APC within the eye are bathed in an environment rich in TGF-P2 [8, 421. Intraocular injection of antigen mobilizes these cells, inducing them to migrate through the trabecular meshwork into the blood, whence they are carried to the spleen [12,[21][22][23]. In the splenic milieu, they present eye-derived antigens to novel populations of specific T and B lymphocytes.…”
Section: Discussionmentioning
confidence: 99%
“…While the immunosuppressive properties of transforming growth factor-p (TGF-8) have usually been examined with respect to the effects of this cytokine on T cells [l-51, there is good evidence to suggest that TGF-8 may suppress T cell activation indirectly, that is, by a primary action on antigen-presenting cells (APC; [6]). This distinction takes on special meaning in certain organs of the body, such as the eye, the brain, and the fetavplacental unit, where immune privilege has been documented, where the local fluids (aqueous humor, cerebrospinal fluid, amniotic fluid) contain significant amounts of TGF-P [7-lo], and where indigenous bone marrow-derived dendritic cells and macrophages reside [11][12][13][14][15].…”
Section: Introductionmentioning
confidence: 99%
“…On the one hand, aqueous humor has been found to inhibit profoundly the activation of primed and effector T cells exposed to rele-[I 165761 nous bone marrow-derived APC, which under the influence of TGF-P, migrate out of the eye across the trabecular meshwork directly into the blood. Upon the arrival of these cells in the spleen [12,[21][22][23], they selectively activate CD8' T cells, B cells that secrete non-complementfixing antibodies, and regulatory T cells that suppress delayed hypersensitivity and complement-fixing antibody formation [24-271. It is pertinent that these eye-derived cells fail to active T cells that effect delayed hypersensitivity. In studying the mechanism of ACAID induction, Wilbanks et al reported that APC from conventional body sites (peritoneal exudate, spleen, blood) can be made to acquire ACAID-inducing properties simply by incubating the cells in vitro with aqueous humor, cerebrospinal fluid, or amniotic fluid [9].…”
Peritoneal exudate cells (PEC) incubated with antigen in the presence of transforming growth factor-(TGF)-beta 2 selectively suppress delayed hypersensitivity and IgG2a antibody production when injected intravenously into naive syngeneic recipients. In this study, we have examined in vitro the effects of TGF-beta 2 on the antigen presenting abilities of PEC to activate DO11.10 T cells that express a transgenic T cell receptor that recognizes ovalbumin peptide fragment 323-339 in the context of I-Ad. PEC were pretreated overnight with TGF-beta 2, washed extensively, then co-cultured with DO11.10 T cells in the presence of native OVA or P323-339. We found that TGF-beta 2-treated PEC induced the production of the T helper type 2 (Th2) cytokine, interleukin-4 (IL-4), but unlike untreated PEC, were unable to stimulate the Th1 cytokines, IL-2 and interferon-gamma (IFN-gamma). Furthermore, TGF-beta 2 was produced in an autocrine fashion by TGF-beta 2-treated PEC and was responsible for this shift to a Th2 response. This conclusion was supported by the following results. First, TGF-beta 2-treated PEC were found to express much more TGF-beta 1 and TGF-beta 2 mRNA than untreated PEC. Second, TGF-beta 2-treated PEC secreted large amounts of TGF-beta including its mature form. Third, addition of neutralizing anti-TGF-beta 2 antibodies, but not neutralizing anti-TGF-beta 1 antibodies, restored the ability of antigen-pulsed, TGF-beta 2-pretreated PEC to stimulate DO11.10 T cells to secrete IL-2 and IFN-gamma. These results indicate that antigen-presenting cells that encounter antigen in a TGF-beta-enriched environment (e.g., in the eye) shift responding native T cells toward Th2 responses by producing TGF-beta during antigen presentation.
“…Williamson et al [1] found contrast sensitivity to be within the normal range with polymethylmethacrylate (PMMA) IOLs. No significant difference was found between the contrast sensitivity with PMMA and silicone IOLs [2] or between PMMA and hy drogel IOLs [3], Bifocal IOLs have shown decreased con trast sensitivity values for intermediate spatial frequencies compared to monofocal IOLs [4], No studies could be found o f contrast sensitivity with silicone IOLs compared to normal eyes.…”
Contrast sensitivity in 64 patients aged from 50 to 69 years with an intraocular lens (IOL) was studied. There were 23 eyes with a silicone and 31 eyes with a polymethylmethacrylate (PMMA) IOL. Ten patients had a silicone IOL in one eye and a PMMA IOL in the other. Contrast sensitivity was examined with the Vistech far vision VCTS 6500 test. The contrast sensitivity test results in silicone and PMMA IOL eyes were in all cpd (cycles per degree) lines significantly worse than in normal eyes except in the 60-year-old group in the 18-cpd line. The contrast sensitivity test results were in all cpd lines better in the silicone IOL eyes than in the PMMA IOL eyes, but it reached significance only in the 3-cpd line. In the 10 patients with the silicone lens in one and the PMMA lens in the other eye, the test results were also better in the silicone IOL eye; it also reached significance only in the 3-cpd line.
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