Browsing by Author "Rao, K N"
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Item Abortion and family planning.(1972-10-16) Rao, K NItem Acinetobacter calcoaceticus infection in and around manipal (Karnataka).(1983-01-01) Kulachandra Singh, M; Kireeti, J; Joseph, A; Subbannayya, K; Stephen, S; Rao, K NItem Advances in tuberculosis research.(1969-05-01) Rao, K NItem Anti-Histone H3.3 G34W antibody is a sensitive and highly specific immunohistochemistry marker for the diagnosis of Giant cell tumor of bone. A validation based on analysis of 198 cases from a single centre in India(Wolters Kluwer - Medknow, 2022-09) Kamble, A; Hui, M; Rao, K N; Narayanan, R; Reddy, B R; Uppin, SG; Chandrasekhar, P.Context: The diagnosis of giant cell tumor of bone (GCTB) is difficult in small biopsies with unusual age of presentation, location, and extensive secondary changes. Most of the GCTBs harbor H3F3A G34W mutations with a subset of cases showing alternate G34V, G34R, and G34L mutations. Objectives: To analyze the expression of anti-histone H3.3G34W antibody in different cellular components of GCTB across different locations and presentations (including the unusual ones) and validate the utility of this antibody in the diagnosis of GCTB and differentiate it from the other osteoclast-like giant-cell-rich lesions. Design: Immunohistochemistry was performed using anti-histone H3.3G34W antibody in the diagnosed cases of GCTB (136 cases of GCTB from 133 patients, including two malignant GCTBs) and other giant cell-containing lesions (62 cases). The presence of unequivocal crisp nuclear staining was considered positive. Results: Immunohistochemistry revealed unequivocal nuclear positivity in the mononuclear cells in 87.3% of the cases of GCTB. Of these, most showed diffuse expression with moderate to strong intensity staining. The positive staining was restricted to the nuclei of mononuclear cells with the nuclei of osteoclastic giant cells being distinctly negative. In addition to conventional GCTBs, two cases each of multicentric and malignant GCTB showed positive staining. The other giant-cell containing lesions were distinctly negative. The present study showed a sensitivity of 87.3% with specificity and positive predictive value of 100%. Conclusion: The anti-histone G34W antibody is a highly sensitive and specific marker for the diagnosis of GCTB and differentiating it from its mimics. The positive staining is restricted to the mononuclear cell component of GCTB with sparing the osteoclastic giant cells further reiterating the fact that the mononuclear stromal cells are the true neoplastic component of GCTB.Item Anticholinergics in myasthenia gravis.(1992-08-01) Rao, K NItem Bromide partition test: a diagnostic criterion for meningitides in children.(1982-03-01) Singhal, S C; Lall, J C; Singh, H; Sood, S C; Rao, K N; Aggarwal, V PItem Bronchopulmonary geotrichosis.(1975-02-01) Rao, K N; Ullal, S R; Stephen, SItem Brucellosis in fowls--a preliminary communication.(1978-11-01) Stephen, S; Indrani, R; Chandrashekara, I; Rao, K NItem Bubble gum story.(1980-11-01) Rao, K N; Shivananda, P GItem Cerebrospinal fluid lactic acid levels in meningitides in children.(1981-12-01) Singhal, S C; Lall, J C; Singh, H; Aggarwal, V P; Rao, K NItem Changing trends in the bacteriology of bone and joint infections.(1977-11-01) Raghava Rao, L V; Chacko, V; Shivananda, P G; Rao, K NItem Comparison of leucocyte migration inhibition and Casoni's skin tests in human hydatidosis.(1981-01-01) Shivananda, P G; Nageshwari, J; Sharada, N R; Rao, K NItem Complement fixation tests in systemic candidiasis.(1981-05-01) Shivananda, P G; Sarvamangala, J N; Elias, A; Rao, K NItem Complement fixing and agglutinating antibodies to Coxiella burnetii in several mammals of Karnataka State.(1979-12-01) Stephen, S; Chandrashekara, I; Rao, K NItem Coproantibody study in Entamoeba histolytica, Entamoeba hartmanni and other parasitic infections.(1985-10-01) Subbannayya, K; Babu, M H; Rao, K N; Shivananda, P GItem Coxiellosis in fowls of Karnataka State.(1980-03-01) Stephen, S; Chandrashekara, I; Rao, K NItem Coxiellosis in reptiles of South Kanara district, Karnataka.(1979-12-01) Stephen, S; Rao, K NItem Critical review of re-orientation of medical education.(1985-04-01) Rao, K NItem Denaturation of pteroylpoly-gamma-glutamyl hydrolase from chicken liver by urea, thiourea and guanidine hydrochloride: altered catalytic properties of the enzyme activated by urea.(1995-02-01) Rao, K NThe effects of varying concentrations of urea, thiourea and guanidine hydrochloride on the enzyme activity and the isoenzymic polypeptide association of pteroylpoly-gamma-glutamyl hydrolase (EC 3.4.22.12) from chicken liver were studied. Incubation of the enzyme at 4 degrees C with low concentrations of the buffered (100 mM sodium acetate containing 1% ascorbate, pH 4.1) solutions of urea (0.55 M) and guanidine hydrochloride (0.05 M) resulted in stimulation (5- and 2-fold respectively) of the activity of the enzyme whereas at higher concentrations of the denaturants (6 M urea, 1 M thiourea or 2 M guanidine hydrochloride) the enzyme was completely inactivated. However, there was no enzyme activation in response to thiorea treatment. Under specific denaturing conditions the association of two isoenzymic polypeptides was studied. The 0.55 M urea- and 0.05 M guanidine hydrochloride-activated enzyme displayed its disaggregated nonidentical polypeptides I and II (M(r) = 41,000 and 17,300 respectively) on Sephadex G-100 gel filtration, SDS-PAGE and sedimentation analyses. The 8 M urea- and 3 M guanidine hydrochloride-inactivated enzyme on the other hand exhibited a single protein aggregate species of an M(r), 57,000 like the native enzyme. Both unmodified native enzyme and the pCMB-modified PtepolyGlu hydrolase responded similarly to these denaturants. The two constituent active polypeptides polyp-I and polyp-II of the heterodimeric gamma-glutamyl glutamyl hydrolase are dissociated in the presence of 0.55 M urea as evident from the PAGE analyses. Some catalytic properties of the activated enzyme were studied and compared with those of the native enzyme. The urea-activated enzyme displayed a shift in the second pH optimum of the double pH-activity profile (optima at pH 4.1 and pH 5.2) from pH 5.2 to pH 6.0. The activated enzyme has a Km value of 0.59 x 10(-6) M (Vmax, 0.10) for 5-CH3-H4PteGlu4 while the native enzyme has the Km of 0.83 x 10(-6) M (Vmax, 0.03) for this substrate. When the reaction mixtures were incubated with the urea-activated gamma-glutamyl hydrolase, a maximum stimulatory effect on the enzyme activity was observed with the bivalent metal ion Ca2+ whereas the most potent inhibitory effect was observed with the trivalent anion citrate.Item Enteropathic Escherichia coli serotypes from various clinical specimens.(1978-10-01) Stephen, S; Indrani, R; Chandrashekra, I; Vaz, A L; Rao, K N
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