scholarly journals Anticataract activity of pioglitazone by using in-Vitro goat lens model

2021 ◽  
Vol 8 (3) ◽  
pp. 208-211
Author(s):  
Rinkal R. Aware ◽  
Hemant J. Pagar ◽  
Ganesh D. Barkade ◽  
Shweta Dhawane
Keyword(s):  
Ascorbic Acid ◽  
Protein Content ◽  
Room Temperature ◽  
Water Soluble ◽  
Time Interval ◽  
Lens Model ◽  
Sodium Potassium ◽  
Water Soluble Protein ◽  
Varied Concentration

In the present study we have selected antioxidants agents like Pioglitazone and Ascorbic acid were subjected for anti-cataract activity by in vitro glucose induced cataract model. In the procedure, goat lenses was incubated along with the aqueous humor solution containing 55mM glucose with Enalpril as a standard compound and Pioglitazone with varied concentration for the time interval of 72 hours at room temperature. There was a formation of blur layer on the goat eyeball occurs after 10-12 hours and this process complete after 72 hours. The cataract inducing lenses showing higher level of Na, MDA (P<0.001) along with the decreases in sodium-potassium ATPase activity and water-soluble protein content. The goat lenses treated with Ascorbic acid 40 µg/ml and Pioglitazone in concentrations of 15, 30, and 60 µg/ml showed increased protein content and prevent the formation of cataract.

scholarly journals The Unique Protein-To-Protein Carotenoid Transfer Mechanism

2017 ◽  
Author(s):  
Eugene G. Maksimov ◽  
Nikolai N. Sluchanko ◽  
Yury B. Slonimskiy ◽  
Kirill S. Mironov ◽  
Konstantin E. Klementiev ◽  
...  
Keyword(s):  
Transfer Process ◽  
Targeted Delivery ◽  
Green Light ◽  
Water Soluble ◽  
Uncharacterized Protein ◽  
Water Soluble Protein ◽  
Orange Carotenoid Protein ◽  
Highly Hydrophobic

Orange Carotenoid Protein (OCP) is known to be an effector and regulator of cyanobacterial photoprotection. This 35 kDa water-soluble protein provides specific environment for keto-carotenoids, the excitation of which induced by the absorption of blue-green light causes dramatic but fully reversible rearrangements of the OCP structure, including carotenoid translocation and separation of C- and N-terminal domains upon transition from the basic orange to photoactivated red OCP form. While recent studies significantly improved our understanding of the OCP photocycle and interaction with phycobilisomes and the fluorescence recovery protein, the mechanism of OCP assembly remains unclear. Apparently, this process requires targeted delivery and incorporation of a highly hydrophobic carotenoid molecule into the water-soluble apoprotein of OCP. Recently, we introduced a novel carotenoid carrier protein, COCP, which consists of dimerized C-domain(s) of OCP and can combine with the isolated N-domain to form transient OCP-like species. Here, we demonstrate that in vitro COCP efficiently transfers otherwise tightly bound carotenoid to the full-length OCP apoprotein, resulting in formation of the photoactive OCP from completely photoinactive species. We accurately analyze peculiarities of this carotenoid transfer process which, to the best of our knowledge, seems unique, previously uncharacterized protein-to-protein carotenoid transfer process. We hypothesize that a similar OCP assembly can occur in vivo, substantiating specific roles of the COCP carotenoid carrier in cyanobacterial photoprotection.

scholarly journals EFFECT OF MANIHOT ESCULENTA AQUEOUS EXTRACT AND THERAPEUTIC ULTRASOUND IN ACCELERATING THE WOUND HEALING PROCESS IN VITRO

2019 ◽  
Vol 81 (4) ◽  
Author(s):  
Ulfah Anwar ◽  
Siti Pauliena Mohd Bohari
Keyword(s):  
Wound Healing ◽  
Ascorbic Acid ◽  
Aqueous Extract ◽  
Manihot Esculenta ◽  
Wound Closure ◽  
Healing Process ◽  
Therapeutic Ultrasound ◽  
Wound Healing Process ◽  
Time Interval

The aim of this research is to investigate the wound healing process in in vitro by combining the Manihot esculenta aqueous extract and therapeutic ultrasound. Firstly, the optimization seeding densities of HSF cell 1184 in six-well plate, and then followed by the scratch assay experiment. The scratched that made was treated with the remedial treatments (Manihot esculenta aqueous extract only; ascorbic acid+ therapeutic ultrasound; Manihot esculenta aqueous extract+ ascorbic acid; Manihot esculenta aqueous extract+ therapeutic ultrasound and also the combination of these three materials). The rate of wound closure was observed and analysed at a time interval of 0, 2, 4, 6, 8, 10 and 24 h by using image J software. Then, the cells viability were analysed using the MTT assay. The result showed that Manihot esculenta aqueous extract coupled with specific dose therapeutic ultrasound represents a significantly high rate of wound closure at 96.10 % with the cell numbers at 5.44×105 cells/mL when compared to the other combination therapy. The finding of this study revealed that Manihot esculenta aqueous extract 200 µg/mL and the therapeutic ultrasound specific dose (3 MHz, 300 mWatt/cm2, 50% in 5 min) have the potential in accelerating wound healing process of cells in in vitro.

Action of Simazine in Increasing Plant Protein Content

Weed Science ◽  
1973 ◽  
Vol 21 (3) ◽  
pp. 233-237 ◽  
Author(s):  
E. L. Pulver ◽  
S. K. Ries
Keyword(s):  
Protein Content ◽  
Soluble Protein ◽  
Time Course ◽  
Nitrate Uptake ◽  
Water Soluble ◽  
Soluble Carbohydrate ◽  
Leucine Incorporation ◽  
Water Soluble Protein ◽  
Time Course Study ◽  
Water Soluble Carbohydrate

Application of 10-8M 2-chloro-4,6-bis(ethylamino)-s-triazine (simazine) to the roots of 10-day old barley (Hordeum vulgareL. ‘Coho’) seedlings grown in nutrient cultures increased the water-soluble protein content when grown at 20 C day, 15 C night with 3 mM nitrate nitrogen. The water-soluble carbohydrate content decreased with increases in water-soluble protein. In a time-course study simazine increased14C-leucine incorporation into protein prior to increasing nitrate uptake, indicating that simazine may have a direct influence on protein synthesis. The nonherbicidal metabolite of simazine, 2-hydroxy-4,6-bis(ethylamino)-s-triazine (hydroxysimazine), did not affect14C-leucine incorporation into protein.

scholarly journals THE PIGMENT-PROTEIN COMPOUND IN PHOTOSYNTHETIC BACTERIA

1940 ◽  
Vol 23 (4) ◽  
pp. 469-481 ◽  
Author(s):  
C. S. French
Keyword(s):  
Ascorbic Acid ◽  
Light Intensity ◽  
Soluble Protein ◽  
Photosynthetic Bacteria ◽  
Water Soluble ◽  
Photochemical Oxidation ◽  
Distilled Water ◽  
Neutral Solution ◽  
Water Suspension ◽  
Water Soluble Protein

1. Photosynthetic bacteria in water suspension break open when treated with supersonic vibration thus liberating the cell contents, including a water soluble protein to which is attached the otherwise water insoluble pigments, bacteriochlorophyll and carotinoids. Both types of pigments appear to be combined with the same protein. 2. The protein pigment compound is insoluble in the region of pH 3.0 to 4.5 and in neutral solution can be completely precipitated by 0.5 saturated (NH4)2SO4. It is soluble in distilled water and adsorbable on fullers' earth. 3. Supersonic extracts of photosynthetic bacteria do not have the ability to carry on photosynthesis, but will act as a photocatalyst for the oxidation of ascorbic acid with visible or infrared radiation. The rate of the photochemical oxidation is proportional to the light intensity.

scholarly journals PENGARUH CARA PEMASAKAN BERBEDA TERHADAP KELARUTAN PROTEIN DAN PERUBAHAN KANDUNGAN KIMIA IKAN SEMBILANG (Paraplotosus albilabris)

2018 ◽  
Vol 46 (2) ◽  
pp. 50
Author(s):  
Siti Rokayah ◽  
Edison Edison ◽  
Sumarto Sumarto
Keyword(s):  
Protein Content ◽  
Soluble Protein ◽  
Nutrient Content ◽  
Proximate Analysis ◽  
Water Soluble ◽  
Fish Meat ◽  
Randomized Design ◽  
Yield Value ◽  
Water Soluble Protein ◽  
Chemical Content

This study aimed to know the value of rendement, chemical content of fresh sembilang fish meat and after experiencing coocking, and water soluble protein and salt soluble protein.   The method used in this research was experimental method with Completely Randomized Design (CRD) which consists of 4 levels of treatment, with R0 (without coocking), R1 (boiling), R2 (boiling with salt), R3 (steaming). The results showed that the average yield value is 47.7% %, in the proximate analysis of fresh sembilang fish meat contains moisture 59.25%, ash 1.42%, fat 6.01%, and protein content 28.39%. The nutrient content of the fish after the cooking differs based on the analysis performed on each treatment R1, R2, R3 has no significant effect on water content, ash content, and protein content, but has significant effect on fat content.Analysis of water soluble protein had a value 4.16%, 3.97%, 3.85% and 3.18.%

scholarly journals The quantification of protein-protein interaction interfaces using solvent-excluded surface-defined properties

2018 ◽  
Author(s):  
Lincong Wang
Keyword(s):  
Protein Interaction ◽  
Protein Complexes ◽  
Protein Docking ◽  
Water Soluble ◽  
Surface Model ◽  
Protein Protein Interaction ◽  
Ring Model ◽  
Water Soluble Protein ◽  
Site Identification

AbstractProtein-protein interaction (PPI) is the cornerstone of nearly every biological process. During last forty years PPI interfaces have been investigated extensively both in vitro and in silico in order to understand both the strength and specificity of PPI. At least three different models, the buried surface model, the O-ring model and the rim- and-core model, have been proposed for PPI interface. However none of them provide much detail about PPI and a single model that reconciles them remains elusive. To identify common physical and geometrical features shared by various PPI interfaces we have analyzed several solvent-excluded surface (SES)-defined properties for a set of well-studied protein-protein complexes with crystal structures. Our analysis shows that the SES-defined properties for the interface atoms of a PPI partner are in general different from those for the surface atoms of a water-soluble protein. Most significantly we find that the partially-buried atoms of a PPI partner have unique SES-defined properties that set them well apart from either the buried atoms or the accessible atoms. Based on distinct SES-defined properties for the accessible, buried and partially-buried atoms shared by various PPI interfaces we propose a new model specified by a list of SES-defined properties shared by various PPI interfaces. Our model is quantitative in nature and should be useful for PPI site identification, protein-protein docking and structure-based design of chemicals targeting PPI.

scholarly journals Nutritional evaluation and transcriptome analyses of short-time germinated seeds in soybean (Glycine max L. Merri.)

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Wei Hu ◽  
Xiaoxue Liu ◽  
Yajun Xiong ◽  
Tingxuan Liu ◽  
Zhan Li ◽  
...  
Keyword(s):  
Protein Content ◽  
Expression Pattern ◽  
Storage Proteins ◽  
Gene Expression Pattern ◽  
Water Soluble ◽  
Regulation Mechanism ◽  
Nutrient Value ◽  
Water Soluble Protein ◽  
Isoflavone Metabolism ◽  
Short Time

AbstractGermination is a common practice for nutrition improvement in many crops. In soybean, the nutrient value and genome-wide gene expression pattern of whole seeds germinated for short-time has not been fully investigated. In this study, protein content (PC), water soluble protein content (WSPC), isoflavone compositions were evaluated at 0 and 36 h after germination (HAG), respectively. The results showed that at 36HAG, PC was slightly decreased (P > 0.05) in ZD41, J58 and JHD, WSPC and free isoflavone (aglycones: daidzein, genistein, and glycitein) were significantly increased (P < 0.05), while total isoflavone content was unchanged. Transcriptomic analysis identified 5240, 6840 and 15,766 DEGs in different time point comparisons, respectively. GO and KEGG analysis showed that photosynthesis process was significantly activated from 18HAG, and alternative splicing might play an important role during germination in a complex manner. Response to hydrogen peroxide (H2O2) was found to be down regulated significantly from 18 to 36HAG, suggesting that H2O2 might play an important role in germination. Expression pattern analysis showed the synthesis of storage proteins was slowing down, while the genes coding for protein degradation (peptidase and protease) were up regulated as time went by during germination. For genes involved in isoflavone metabolism pathway, UGT (7-O-glucosyltransferase) coding genes were significantly up regulated (40 up-DEGs vs 27 down-DEGs), while MAT (7-O-glucoside-6′′-O-malonyltransferase) coding genes were down regulated, which might explain the increase of aglycones after germination. This study provided a universal transcriptomic atlas for whole soybean seeds germination in terms of nutrition and gene regulation mechanism.

scholarly journals Structurally Normal Corneas in Aldehyde Dehydrogenase 3a1-Deficient Mice

2002 ◽  
Vol 22 (3) ◽  
pp. 849-855 ◽  
Author(s):  
David W. Nees ◽  
Eric F. Wawrousek ◽  
W. Gerald Robison ◽  
Joram Piatigorsky
Keyword(s):  
Protein Content ◽  
Corneal Epithelium ◽  
Soluble Protein ◽  
Water Soluble ◽  
Null Mouse ◽  
Wild Type ◽  
Water Soluble Protein ◽  
Slit Lamp Microscopy ◽  
Deficient Mice

ABSTRACT We have constructed an ALDH3a1 null mouse to investigate the role of this enzyme that comprises nearly one-half of the total water-soluble protein in the mouse corneal epithelium. ALDH3a1-deficient mice are viable and fertile, have a corneal epithelium with a water-soluble protein content approximately half that of wild-type mice, and contain no ALDH3a1 as determined by zymograms and immunoblots. Despite the loss of protein content and ALDH3a1 activity, the ALDH3a1−/− mouse corneas appear indistinguishable from wild-type corneas when examined by histological analysis and electron microscopy and are transparent as determined by light and slit lamp microscopy. There is no evidence for a compensating protein or enzyme. Even though the function of ALDH3a1 in the mouse cornea remains unknown, our data indicate that its enzymatic activity is unnecessary for corneal clarity and maintenance, at least under laboratory conditions.

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