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P Mishra

Publications and source records attributed to P Mishra.

At least 19 recordsLinked to original sources
PubMed1998

Differentiation of malignant and degenerative benign bone disease using Tc-99m MDP and Tc-99m citrate scintigraphy.

The authors present a prospective analysis of Tc-99m MDP and Tc-99m citrate scintigraphy in 108 patients with known malignant or degenerative benign bone disease. Of 108 patients, 59 (group A) had malignant bone disease. The other 49 patients (group B) had degenerative benign bone disease for which the results of Tc-99m MDP scans were positive. In both groups the Tc-99m citrate scan was performed 1 week after the Tc-99m MDP scan. The Tc-99m citrate/Tc-99m MDP lesion-to-background radioisotope uptake ratio (RUR) was calculated for each lesion 3 hours after radionuclide administration. The mean RUR for the malignant lesions was 1.0 +/- 0.484; for the benign lesions, the RUR was 0.29 +/- 0.250. Static imaging was also done for 10 lesions each from the malignant and benign groups at 1, 3, and 24 hours to study the kinetics of Tc-99m citrate. Time-activity curves for malignant lesions showed that the RUR remained high for 24 hours, whereas benign lesions showed a drastic decrease at 3 and 24 hours compared with the 1-hour images. The ratio of Tc-99m citrate to Tc-99m MDP is a promising parameter to differentiate malignant from benign degenerative lesions seen as areas of increased activity on Tc-99m MDP bone scans. The sensitivity and specificity of this technique were 97.8% and 95%, respectively.

Adult↗
PubMed1996

Scintiscan demonstration of localized bowel loop inflammation. Comparison of Tc-99m dextran, Tc-99m citrate, and Tc-99m human immunoglobulin G.

A 60-year-old man with localized small bowel inflammation underwent abdominal scintigraphy with Tc-99m human polyclonal immunoglobulin G and two experimental inflammation-seeking agents, Tc-99m dextran and Tc-99m citrate. The abnormal loop was visualized in all the three studies. Additionally, the Tc-99m dextran study revealed exudation and luminal transit of the tracer suggestive of regional protein-losing enteropathy. The authors conclude that Tc-99 dextran and Tc-99 citrate are clinically suitable inflammation-seeking agents that need further evaluation, especially for locating abdominal inflammations.

Citrates↗
PubMed1996

A kit for the instant preparation of 99Tcm-citrate for tumour and inflammation scintigraphy.

A lyophilized kit has been developed to produce 99Tcm-citrate (99%) instantly when mixed with 99TcmO4-. The ingredients of the kit, citrate and stannous chloride, are in a ratio of 100:1 (w/w) and are bound to 700 MBq 99Tcm, sufficient for use in a single patient. The shelf life of the kit when kept refrigerated is at least 3 months. The blood clearance and organ distribution of 99Tcm-citrate have been studied in rabbits and mice respectively, showing its fast clearance (55% at 5 min) and low uptake by the reticulo-endothelial system and other organs. The main route of clearance is via the kidneys. Scintigraphic studies in experimental mice have demonstrated high levels of accumulation of 99Tcm-citrate in turpentine-induced abscess (target-to-non-target ratio 4.2:1) and EAT implanted tumour in mice (T/NT 5:1) 1 h after its administration. In keeping with these animal studies, low uptake of 99Tcm-citrate by normal organs and fast blood clearance have been demonstrated in human patients with infection and tumour as early as 5 min post-administration. This study documents a new kit developed for the preparation of 99Tcm-citrate suitable for the scintigraphic assessment of abscess, infection and tumour.

Abscess↗
PubMed1995

Fourier-transform infrared spectroscopic investigation of protein stability in the lyophilized form.

Upon the removal of water, proteins undergo a major, reversible rearrangement of their secondary structure, as revealed by FTIR spectroscopy. We have found herein that for recombinant human albumin (rHA) the extent of this structural change does not depend significantly either on the composition of the aqueous solution prior to lyophilization (protein concentration, pH, and the presence of excipients such as dextran or NaCl) or on the mode of dehydration (lyophilization, spray drying, or rotary evaporation), even though these factors profoundly affect rHA's solid-state stability against moisture-induced aggregation. In all cases, the alpha-helix content of rHA drops from 58% in solution to 25-35% in the dehydrated state, the beta-sheet content rises from 0 to 10-20%, and unordered structures increase from 40% to 50-60%. We have also investigated another model protein, hen egg-white lysozyme, and confirmed that it too undergoes a significant alteration of the secondary structure upon lyophilization. The extent of this structural reorganization has been found to be insensitive to the pH of the aqueous solution prior to lyophilization from pH 1.9 to 5.1, even though the thermal transition temperature (Tm) in aqueous solution over this range varies by 30 degrees C.

Dextrans↗
PubMed1994

A simplified kit for instant preparation of technetium-99m human immunoglobulin-G for imaging inflammatory foci.

A kit consisting of reduced human immunoglobulins G (hIgG), methylene diphosphonate, stannous chloride and ascorbic acid has been developed to instantly produce technetium-labelled hIgG of greater than 97% purity and suitable for inflammation foci scintigraphy in patients. The shelf life of the kit when stored at 4-7 degrees C was at least 3 months. 99mTc-hIgG prepared from the kit, when incubated at 37 degrees C for 24 h in physiological saline and human serum was found to degrade by only 7.8 and 4.3%, respectively, thereby indicating high stability of the labelled product. Competitive RIA data did not exhibit loss of immunoreactivity of the hIgG due to its reduction. Blood clearance of the radiopharmaceutical in rabbits exhibited a monophasic exponential pattern. Biodistribution in mice showed uptake by liver (4.93%), kidneys (3.07%) and intestines (2.12%) at 4 h which was reduced to 1.99, 2.18 and 1.93%, respectively at 24 h. Radiolabelled hIgG prepared from the kit was found to be quite satisfactory for inflammation scintigraphy in human patients.

Animals↗
PubMed1994

A novel method for labelling human immunoglobulin-G with 99Tcm suitable for inflammation scintigraphy.

An amount of 1.0 mg human immunoglobulin G (hIgG) treated with ascorbic acid at a molar ratio of 1:5000 for 16 h at 4-7 degrees C was mixed with 250 micrograms GHA and 5 micrograms stannous chloride dihydrate in normal saline. Radiolabelling of hIgG (> 98%) was achieved instantly when mixed with 99Tcm-pertechnetate. The preparation was sufficiently stable in serum at 37 degrees C. The competitive binding assay and gel electrophoresis of the native and reduced hIgG did not show any measurable loss in immunoreactivity and intactness due to its reduction. There was no significant decrease in the radiolabel of labelled hIgG when incubated with diethylenetriaminepentaacetate (DTPA) (50-fold), in contrast with about 9% loss of the radiolabel by treating it with a similar concentration of cysteine. Blood clearance of labelled hIgG in rabbits was biphasic with about 78 min and 8 h as T1/2 of the fast and slow phases. Biodistribution of the radiotracer in mice at 4 h showed its uptake by liver (10.2%), kidneys (5.39%), intestines (7.33%) and muscles (3.9%), which altered to 5.63, 3.20, 4.03 and 6.73%, respectively, at 24 h. The radiotracer was excreted through both renal and hepatobiliary routes. High accumulation of the radiolabelled hIgG in inflammatory lesions of the patients confirmed the clinical usefulness of the method developed.

Animals↗
PubMed1994

Differential increase in cytoplasmic pH at bud and germ tube formation in Candida albicans: studies of a nongerminative variant.

The changes in cytoplasmic pH (pHi) accompanying the morphological transition of Candida albicans were studied using a nongerminative variant. A transient cytoplasmic alkalinization at the time of evagination was observed in both the variant and its parent. Under zinc-deficient conditions the wild-type cells that formed buds at pH 4.5 and mycelia at pH 6.5 showed an increase in pHi of 0.58 and 0.12 pH units, respectively. Under similar conditions the pHi of the nongerminative variant that formed buds at both pH 4.5 and 6.5 increased by 0.66 and 0.40 pH units, respectively, suggesting that a greater magnitude of increase in pHi at the time of evagination is probably needed for bud formation. These results provide evidence for a correlation between intracellular alkalinization and time of cell differentiation in C. albicans.

Candida albicans↗
PubMed1992

Emerging role of lipids of Candida albicans, a pathogenic dimorphic yeast.

It is clear that C. albicans lipids have gained tremendous importance in recent years. In addition to being a barrier for entrance of various metabolites, it also provides the site of action for the synthesis of enzyme(s) involved in cell wall morphogenesis and antifungal action. While alterations in lipid composition during a yeast to mycelia transition have been observed, in most of the studies, lipid fluctuations reported could have been due to various environmental factors involved in the induction of morphogenesis [4,5]. A clear understanding of lipid biosynthesis and metabolic blocks due to antifungal action is likely to shed further light on selective interactions of antifungals. Despite the multifacet role of lipids in various functions of this pathogenic yeast, their exact involvement is poorly understood. The situation is little better with regard to ergosterol and its metabolism. Ergosterol is, indeed, important for anti-candidal activity and appears to be involved in the morphogenesis of C. albicans. The fluctuation in phospholipid composition have led to altered properties of plasma membrane namely, membrane fluidity, transport activities and drug sensitivity, which suggest that-a critical level of individual phospholipid is important for proper functioning of the plasma membrane. What the exact role is of individual phospholipid is far from clear. Many unanswered questions relating to the role of PI and sphingomyelin in signal transduction, involvement of phospholipases in the maintenance of phospholipid composition, and role of lipid transfer proteins in assembly and asymmetry of lipids are some aspects which merit further work.

Candida albicans↗
PubMed1992

Pharmacological screening of few new 2-(substituted acetyl) amino-5-alkyl-1,3,4-oxadiazoles.

Nine new 2-(substituted acetyl) amino-5-alkyl-1,3,4-oxadiazoles were synthesised and confirmed on the basis of IR and nitrogen analysis. These were screened for spasmolytic, anti-inflammatory and their effects on blood pressure after determining ALD50. Compounds GK-4 i.e. 2-(diethylaminoacetyl)- amino-5-methyl-1,3,4-oxadiazole and GK-8 i.e. 2-(din-propylamino acetyl)-amino-5-ethyl-1,3,4-oxadiazole were found to be spasmolytic. Compound GK-6 i.e. 2-(diethylaminoacetyl)-amino-5-n-propyl-1,3,4-oxadiazole was found to be a potent hypotensive agent with the effect lasting for more than two hours.

Animals↗
PubMed1991

Amino acid uptake as a function of differentiation in Candida albicans: studies of a non-germinative variant.

The transport of four amino acids (L-methionine, L-phenylalanine, L-lysine and L-alanine) was studied during pH-regulated dimorphism in Candida albicans and its stable, non-germinative variant. The permeases responsible for uptake responded differently to differentiation and the transport activities varied during the course of morphogenesis. An increase in uptake around the time of evagination was observed in all four amino acids in both the strains studied. The uptake rates of L-methionine and L-phenylalanine were greater in fully differentiated hyphae, while the rate of L-lysine was higher in fully differentiated buds. Uptake rates of L-alanine, however, did not show any morphotypic related variation. The possible implication of these transport activities in relation to differentiation is discussed.

Alanine↗
PubMed1991

Dimorphism-associated changes in plasma membrane H(+)-ATPase activity of Candida albicans.

In situ plasma membrane H(+)-ATPase activity was monitored during pH-regulated dimorphism of Candida albicans using permeabilized cells. ATPase activity was found to increase in both the bud and germ tube forming populations at 135 min which coincides with the time of evagination. Upon reaching the terminal phenotype the mycelial form exhibited higher H(+)-ATPase activity as compared to the yeast form. At the time of evagination H(+)-efflux exhibited an increase. K+ depletion resulted in attenuated ATPase activity and glucose induced H(+)-efflux. The results demonstrate that ATPase may play a regulatory role in dimorphism of C. albicans and K+ acts as a modulator.

Candida albicans↗