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Introduction: Cissus quadrangularis is a popularly known traditionally used medicinal plant from ancient times. The common name of cissus quadrangularis in tamil 'pirantai'. This plant has been consumed as a vegetable and easily available plant. The plant is used to heal the many sorts of diseases including stroke, epilepsy, bone related diseases, skin infections, constipation, piles, anemia, burns, wounds and diabetes also. The present study was hypothesized to evaluate the effects of anti-hyperglycemic activity of stem cissus quadrangularis on Streptozotocin induced diabetic rats. Materials and Methods: The animals are divided into 5 groups, each group contain 6 animals. Group I- control. Group II -STZ induced negative control. Group III- STZ induced rats treated with metformin. Group IV& V -STZ induced rats treated with (200 and 400 mg/kg) ethanol extract. After overnight fasting, a single dose of STZ (40 mg/kg) were given by intraperitoneally. After confirmation of diabetes the ethanolic extract of cissusquadrangularis 200 mg and 400 mg were given orally. Results: This study reveals that cissusquadrangularis have more effects in reducing blood sugar level in diabetic rats. The results shows that 400mg/kg/bw CQ have significant effects then with 200 mg/kg/bw. The entire study concluded diabetic patients are prone to wound and related diseases. Conclusion: Conception of cissus quadrangularis are more effective drug to reduce the blood sugar levels and also heal diabetic wounds. [ABSTRACT FROM AUTHOR]

Background: Orbitofacial anthropometric measurements can be used in identification of gender and ethnicity in forensic anthropology. It also plays a crucial role used in plastic surgery and for identifying genetic syndromes. Canthus is the term employed to explain the either corner of the eyes. Inner canthus is also called as medial or nasal canthus. Outer canthus, is otherwise called as lateral or temporal canthus. Normal canthal values can function as a guide for the diagnosis of pathology and interventions for craniofacial abnormalities. Thus, it is necessary to have a knowledge about the local data of those parameters since this standard reflects the doubtless different pattern of craniofacial growth resulting from racial, ethnic, sexual and dietary differences. Hence this study is undertaken to find out the normative inner canthal and outercanthal distance measurement in population of South Indian region. Aims and Objectives: The present study was done to find out the normal inner and outercanthal distance and also canthal index of population of South Indian ethnic origin and also to analyse the sexual dimorphism in them. Materials and Method: This descriptive cross-sectional study was conducted on 200 volunteers of age group 18-25 years of both sexes belonging to South Indian region. Innercanthal distance(ICD) and Outer canthal distance(OCD) were measured using digital vernier caliper. Canthal index was calculated. All the data were analysed using SPSS 16.0 version software and correlated with gender. Results: Mean innercanthal distance was found to be 2.64 ±0.51 cm in males and 2.51 ±0.46 cm in females respectively in the present study. There is significant sexual dimorphism in ICD. The study also showed outercanthal distance to be 10.35± 0.81cm in males and 10.19 ±1.02 cm in females respectively. Canthal index was 25.71 ±4.91 in males and 24.83±7.83 in females. There is no significant sexual dimorphism in OCD and Canthal index. Conclusion: It was observed that all the values were significantly higher in males than females of south Indian ethnic origin. And there is a significant sexual dimorphism in inner intercanthal distance. [ABSTRACT FROM AUTHOR]

Presents information on a study which incorporated the p-phenylenebenzobisthiazole polymer with electron lamines, electroactive triarylamino. Details on the experiment; Results and discussion; Conclusions.

Passive methods of controlling shock/boundary-layer interactions (SBLIs) consist of a porous surface covering a cavity or a plenum located in the region of the SBLI. The present study focuses on the flowfield downstream of a Mach 1.42 SBLI controlled with various passive devices such as a conventional porous plate, a microporous plate, streamwise slots, a conventional mesoflap array, and a hybrid flap array. Qualitative analysis of the flowfield for the various control devices investigated was achieved with spark shadowgraph visualizations and surface oil-flow visualizations. Quantitative analysis was accomplished by measuring surface static pressure distributions and boundary layer velocity profiles. The flowfields downstream of the slot-controlled and hybrid flap array-controlled SBLIs were found to be highly three-dimensional, whereas the flowfields were predominantly two-dimensional for the remainder of the control devices. It was found that only the conventional mesoflap array had an improved total pressure recovery compared to the baseline solid wall. [ABSTRACT FROM AUTHOR]

Poly(arylene ether pyrazole)s containing N–H and N-phenyl groups have been prepared by the aromatic nucleophilic displacement reaction of two new bisphenols containing a pyrazole ring with activated aromatic dihalides in N,N-dimethylacetamide at 155 °C in the presence of anhydrous potassium carbonate. The polymers exhibited glass transition temperatures (Tg) ranging from 190–296 °C and inherent viscosities from 0.44–1.96 dl g−1. Poly(arylene ether-pyrazole)s containing N–H groups exhibited higher Tg and mechanical properties than the corresponding N-phenyl-containing poly(arylene ether pyrazole)s. The chemistry, physical and mechanical properties of these polymers are discussed. [ABSTRACT FROM PUBLISHER]

During our routine postmortem examination, we found a female infant with "True Cyclopia." The two entire eye balls had fused completely to form one midline organ. The infant was a female who weighed 2910 g. The gestation period was 35 weeks. Infant lived for a short period of less than 20 minutes. The birth was a product of a 4th pregnancy. [ABSTRACT FROM AUTHOR]

A kinetic analysis of the decarboxylation of malonyl-CoA and the condensation--CO2 exchange reaction of fatty acid synthesis has been carried out. The analysis supported by experimental evidence defines conditions under which the decarboxylation of malonyl-CoA quantitatively reflects the activity for the condensation reaction between enzyme-bound acyl and malonyl groups. NADP+ decreases the release of 14CO2 from radiolabeled malonyl-CoA by lowering the rates of the processes leading to the formation of triacetic acid lactone. For accurate measurements, the enzyme concentration should be less than 200 micrograms/mL, and malonyl-CoA/enzyme ratios should be 200 or less. Short reaction periods (1 min or less) and inclusion of NADP+ (100 microM) enhance the accuracy of measurements. These analyses have been used to explain the mechanism of malonyl-CoA mediated inactivation of chicken liver fatty acid synthetase and are appropriate for determining the functional condensing site of the polyfunctional polypeptide chains comprising the dimeric enzyme.

The kinetics of high affinity heparin binding to human antithrombin III has been studied by stopped flow fluorimetry, using the 40% antithrombin fluorescence enhancement resulting from this interaction. At mu 0.15, pH 7.4, and 25 degrees C, the observed pseudo-first order rate constant varies hyperbolically with heparin concentration with a limiting rate constant of 440 +/- 90 s-1, demonstrating that heparin binding is a two-step process involving a conformational change in antithrombin III. An identical dependence is produced when antithrombin is varied, consistent with a symmetrical mechanism in which heparin binding induces a conformational change in antithrombin rather than perturbing an equilibrium between two conformational states of the protein. The rate constant for dissociation of the antithrombin-heparin complex is 1.1-1.5 s-1 at mu 0.15, as determined from the ordinate intercept at low heparin concentrations or by dissociation of the antithrombin-heparin complex with iodide. Observation of a single pseudo-first order binding rates over a 400-fold heparin concentration range with no detectable lags is compatible with the initial binding step being in rapid equilibrium with a KD of 4.3 +/- 1.3 X 10(-5) M at mu 0.15. Variation in ionic strength primarily affects the KD for the initial binding step with little effect on the conformational change rate constants, implying that binding involves ionic interactions. Calculation of the overall dissociation equilibrium constant from these rate parameters agrees with the directly determined value of 7.2 +/- 1.9 X 10(-8) M at mu 0.15. A major function of the conformational change is, thus, to increase the affinity of heparin for antithrombin III greater than 300-fold. The implications of these findings for the mechanism of the heparin-catalyzed inhibition of coagulation proteases by antithrombin III are discussed.

Structural and conformational organization of chicken liver fatty acid synthetase has been probed using its fluorescent coenzyme, NADPH. Three NADPH binding sites per mole of the enzyme complex, of apparently identical dissociation constant (KD = 0.6 muM) can be titrated at temperatures above 12 degrees. These results are in disagreement with the earlier studies of Hsu and Wagner (Hsu, R. Y., and Wagner, B. J. (1970) Biochemistry, 9, 245-251) in which four such sites could be titrated. At 12 degrees, the composite sites split into two subsets: a pair of sites with a KD of 0.3 muM and a third site with a Kd of 1.1 muM. At lower temperatures (5 degrees or 2 degrees), the site with weak affinity disappears, leaving a pair of sites with a Kd of 0.5 muM. Similar observations were made when the enzyme was modified with phenylmethylsulfonyl fluoride, a specific and selective inhibitor of fatty acyl-CoA deacylase (s) of the pigeon liver enzyme complex (Kumar, S. (1975) J. Biol. Chem. 250, 5150-5158). Partial modification with phenylmethylsulfonyl fluoride elicits a NADPH binding response similar to the binding observed at 12 degrees, i.e. two sets of binding sites with nonidentical dissociation constants. Further modification corresponding to the complete loss of deacylase function results in a set of two apparently identical binding sites, and the third site is not available for titration. The modified enzyme retains the two reductase functions as measured by the model substrates, acetoacetyl-N-acetylcysteamine and crotonyl-CoA. Furthermore, the addition of acetyl- and malonyl-CoA (100 muM each) to the modified enzyme lowers the NADPH binding affinity by a factor of 3. Other observations show that the quantum yield, as measured by the ratio of fluorescence intensity of bound and free NADPH, changes with temperature and ionic strength. Lowering the temperature from 30 degrees to 2 degrees increases the enhancement ratio by 50%, whereas increase in ionic strength from 0.05 to 0.2 M potassium phosphate lowers it to 50% of the original level. Measurement of NADPH binding in the presence of NADP+, NADH, NAD+ and adenosine-2'-monophospho-5'-diphosphoribose demonstrates that NADP+ shows competitive behavior for NADPH sites (KD = 10.6 muM), whereas NADH and NAD+ show noncompetitive (KD (apparent) = nearly 600 muM) and rather complicated interactions implicating nonspecific conformational alteration of the enzyme complex. The behavior of adenosine 2'-monophospho-5'-diphosphoribose is intermediate between NADP+ and NADH. These data are discussed in terms of substrate-mediated conformational changes and the moles of each of the reductase enzymes per mole of the enzyme complex, the polarity of the NADPH binding region, and the probable structure of the nicotinamide moiety when bound to the enzyme.

This article describes a method for the chemical immobilization of concanavalin A (Con A) on the inside wall of a single hollow cellulose fiber for use in glucose affinity sensor. Periodate oxidation of cellulose fiber followed by a spacer for Con A attachment was deemed to be the most optimal procedure for achieving the highest sensitivity of the sensor without compromising its physical integrity. The effects of variables like the duration of periodate oxidation and its concentration and pH of the spacer coupling step and its duration have been examined. The mechanical strength of the hollow fiber as well as its permeability to the analyte (glucose) have been evaluated prior to and after Con A coupling process. It has been demonstrated that Con A bound hollow fiber prepared according to the procedure outlined here can be successfully used to construct glucose affinity sensor for operation in the physiological range of glucose concentrations.

Chicken liver fatty acid synthetase complex is irreversibly inactivated by one of the substrates, malonyl-CoA. Acetyl-CoA has a dual role. At concentrations less than or comparable to those of malonyl-CoA, the rate of inactivation is enhanced, whereas at acetyl-CoA/malonyl-CoA ratios greater than 2, the rte of inactivation is slowed down. NADP+ at low concentrations (25 microM) affords considerable protection against malonyl-CoA mediated inactivation whereas NAD+ even at 1.0 mM concentration has no effect. The inactivation process does not lead to the dissociation of the enzyme complex and is accompanied by subtle conformational changes as measured by circular dichroism measurements. Of all the model partial reactions, decarboxylation of malonyl-CoA and the condensation--CO2 exchange are the only reactions which are not catalyzed by the modified species. The process of inactivation is accompanied by enhanced covalent binding of malonyl groups such that approximately 6 mol of the acyl group is bound per mol of the enzyme at complete inactivation. The available evidence suggests that the inactivation of the enzyme results from the binding of malonyl group(s) at or near the condensing site of the enzyme.