Group A streptococci resistant to erythromycin & lincomycin.
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Biomedical subjects
Publications and source records attributed to K Prakash.
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We have identified a 110-kDa pI 5.6 phosphoprotein with DNA binding properties in the rat pachytene spermatocyte nuclear matrix. By immunoblotting and indirect immunofluorescence assays using polyclonal antibodies against the 110-kDa protein, we observed that it was germ cell nuclear matrix specific, more prominent in pachytene spermatocytes compared to premeiotic spermatogonia or postmeiotic round spermatids, and present in rat oocytes and in germ cells of mouse and monkey. We propose that this protein could play an important role in the meiotic process.
A coagglutination test for detection of group A streptococci in throat samples was evaluated in a multicentre study and found to be about 95% sensitive when applied to swabs taken from symptomatic patients which yielded more than 100 colonies per plate on culture. The sensitivity of the test dropped significantly when it was applied to swabs giving fewer than 100 colonies on culture. The specificity of the test was high regardless of colony count on conventional media.
T cell subsets were studied in 45 patients, 15 each of acute rheumatic fever, rheumatic heart diseases, and acute glomerulonephritis and compared with 10 normal control in the same age group. A significant depression in the OKT1 and OKT4 +ve cells and insignificant increase in the OKT8 +ve cells was noted in all these groups of cases.
Thirty patients with acute rheumatic fever, and 20 with inactive rheumatic heart disease were studied in order to determine parameters which differentiate the two groups. Subcutaneous nodules developed following the subcutaneous injection of autologous blood in 16 of 26 patients with rheumatic fever but in none of the 20 with inactive rheumatic heart disease (P = 0.00001). Myocardial reactive antibodies were found in 14 of 30 patients with rheumatic fever, and in 4 of 20 with inactive rheumatic heart disease (P = 0.0505). Significantly higher values of IgG (P less than 0.001), IgA (P less than 0.01), C3 (P less than 0.001) and C4 (P less than 0.001) were observed in rheumatic fever patients. There was no significant difference in IgM levels. A combination of three variables (artificial subcutaneous nodules, IgA, and C3) had a sensitivity of 87% and a specificity of 100% for rheumatic fever. A combination of two variables (artificial subcutaneous nodules and IgA) had a sensitivity of 84% and a specificity of 100% for rheumatic fever.
A total of 171 isolates of Streptococcus pneumoniae were obtained from eyes of children who had congenital dacryocystitis, congenital cataract and glaucoma, acute bacterial conjunctivitis, corneal ulceration, nasolacrimal duct block, or discharging socket, or who had developed ectropion, endophthalmitis and orbital cellulitis. The highest number of strains was obtained from cases of dacryocystitis (74.4%), followed by conjunctivitis (8.2%) and those having developed nasolacrimal duct block (7.6%). The least overall resistance was to erythromycin (17.6%) and chloramphenicol (31.0%). Erythromycin being unavailable for ocular use in India, chloramphenicol was reported to be one of the best drugs against pneumococcal ocular infections in children, the other being cloxacillin, a 2.5% solution of which is made from injectable cloxacillin and used as an ophthalmic preparation. Their use on patients has met with considerable success. Nineteen out of 20 isolates were typeable--the types being 3, 46, 8, 28, 29, 45, 21 and 18. To the best of our knowledge, this is the first report from a developing country of serotyping ocular strains of pneumococci.
Ribophorins I and II are two transmembrane glycoproteins that are characteristic of the rough endoplasmic reticulum and are thought to be part of the apparatus that affects the co-translational translocation of polypeptides synthesized on membrane-bound polysomes. A ribophorin I cDNA clone containing a 0.6-kb insert was isolated from a rat liver lambda gtll cDNA library by immunoscreening with specific antibodies. This cDNA was used to isolate a clone (2.3 kb) from a rat brain lambda gtll cDNA library that contains the entire ribophorin I coding sequence. SP6 RNA transcripts of the insert in this clone directed the in vitro synthesis of a polypeptide of the expected size that was immunoprecipitated with anti-ribophorin I antibodies. When synthesized in the presence of microsomes, this polypeptide, like the translation product of the natural ribophorin I mRNA, underwent membrane insertion, signal cleavage, and co-translational glycosylation. The complete amino acid sequence of the polypeptide encoded in the cDNA insert was derived from the nucleotide sequence and found to contain a segment that corresponds to a partial amino terminal sequence of ribophorin I that was obtained by Edman degradation. This confirmed the identity of the cDNA clone and established that ribophorin I contains 583 amino acids and is synthesized with a cleavable amino terminal insertion signal of 22 residues. Analysis of the amino acid sequence of ribophorin I suggested that the polypeptide has a simple transmembrane disposition with a rather hydrophilic carboxy terminal segment of 150 amino acids exposed on the cytoplasmic face of the membrane, and a luminal domain of 414 amino acids containing three potential N-glycosylation sites. Hybridization measurements using the cloned cDNA as a probe showed that ribophorin I mRNA levels increase fourfold 15 h after partial hepatectomy, in confirmation of measurements made by in vitro translation of liver mRNA. Southern blot analysis of rat genomic DNA suggests that there is a single copy of the ribophorin I gene in the haploid rat genome.
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Effects of harmaline and ouabain on intestinal transport in vitro of D-glucose in the pigeon are investigated. Harmaline inhibits glucose influx and affects intestinal Na+-K+-ATPase activity though the substrate uptake is more sensitive than the enzyme activity. Low concentration of harmaline while drastically inhibiting glucose uptake, does not affect intracellular concentration of Na+ and K+. In contrast, ouabain, though has no significant effect on glucose uptake, alters substantially the ionic balance of cells. Harmaline also affects that component of nutrient influx which is left unaffected by ouabain. Mucosal-serosal flux of glucose is reduced by harmaline when it is present only on the mucosal side of everted intestinal sacs. On the contrary, similar effect is produced by ouabain when it is placed only on the serosal side. It appears that harmaline possibly inhibits glucose transport in the pigeon intestine by two ways: first, by irreversible binding Na+-K+-ATPase - a feature shared by ouabain, and second, by reversible binding Na+-binding sites of enterocyte membrane - an effect not shared by ouabain.
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