scholarly journals Study of Potential Application of Cyanobacteria Leptolyngbya Valderiana in Skin Cosmeceuticals

2021 ◽  
Vol 6 (04) ◽  
pp. 44-49
Author(s):  
Shraddha Ratnaparkhe ◽  
Devyani Mali ◽  
Bela Nabar
Keyword(s):  
Salicylic Acid ◽  
Radical Scavenging ◽  
Cell Extract ◽  
Antioxidant Potential ◽  
Tree Bark ◽  
Tyrosinase Inhibition ◽  
Isolation And Identification ◽  
Skin Whitening ◽  
Whole Cell ◽  
Whole Cell Extract

Skin is the outermost cover and first line of defense of the human body. Skin cosmeceuticals are therapeutic agents used to maintain flawless skin and prevent skin disorders. Considering the ill effects of synthetic active agents, natural metabolites are preferred for skincare. Cyanobacterium was known to produce various secondary metabolites with therapeutic potential. This study focuses on screening whole-cell extract of Leptolyngbya valderiana for skincare. Isolation and identification of cyanobacteria were made. The whole-cell extract of Leptolyngbya valderiana was studied for its metabolite profile, mainly for proteins, carbohydrate, and lipid content. Screening of whole-cell extract was carried out for its (2,2’-azino-bis (3-ethylbenzothiazoline-6-sulfonic acid)) (ABTS) radical scavenging ability and UV absorption potential. The antimicrobial effect of extracts was determined by agar cup and minimum inhibitory concentration (MIC) method using salicylic acid as a standard. Skin whitening potential was determined using tyrosinase inhibition assay. Leptolyngbya valderiana was isolated from the tree bark and selected for further study. The extract of Leptolyngbya valderiana was found to have 25.22% proteins, 36.65 % carbohydrates and 35.97% lipids. The extract was found to have antioxidant potential with 96.55% ABTS radical scavenging potential. Antimicrobial potency of the extract against Staphylococcus aureus ATCC 6538, Propionibacterium acne MTCC 1351, Candida albicans ATCC 10231 was equivalent to salicylic acid. The test extract was found to inhibit the tyrosinase enzyme by 43.46%. The test extract is rich in proteins, carbohydrates, and lipids. The extract has significant antioxidant potential, antimicrobial efficiency, ability to absorb ultraviolet B and ultraviolet A region, tyrosinase inhibition potential indicative photoprotective, and skin whitening potential. The isolate Leptolyngbya valderiana has a promising potential for skin cosmeceuticals.

scholarly journals Chromatin assembly in a yeast whole-cell extract

1997 ◽  
Vol 94 (17) ◽  
pp. 9034-9039 ◽  
Author(s):  
M. C. Schultz ◽  
D. J. Hockman ◽  
T. A. A. Harkness ◽  
W. I. Garinther ◽  
B. A. Altheim
Keyword(s):  
Cell Extract ◽  
Chromatin Assembly ◽  
Whole Cell ◽  
Whole Cell Extract

scholarly journals Effect of Calcium Carbide on Rat Tissue

1970 ◽  
Vol 6 (2) ◽  
pp. 93-98 ◽  
Author(s):  
Younus Patoare ◽  
Md Iqbal Hossain ◽  
Mohammad Nurul Islam ◽  
Akhtarunnessa Chowdhury ◽  
Seheli Parveen ◽  
...  
Keyword(s):  
Acid Phosphatase ◽  
Calcium Carbide ◽  
Cell Extract ◽  
Control Group ◽  
Histopathological Study ◽  
Histopathological Analysis ◽  
Whole Cell ◽  
Group I ◽  
Collecting Tubules ◽  
Whole Cell Extract

To evaluate the effects of Calcium carbide (CaC2) in biological system, an in vivo study was carried out on Long Evans rats. CaC2 was administered orally once daily for one month with specific concentrations. Group- I was considered as the control group (without CaC2), Group - II, III, IV and V were the sample groups treated with CaC2 having concentration of 1g/kg, 2g/kg, 5g/kg and 10g/kg body weight respectively. The experiment was conducted to detect any cellular and molecular level changes caused by CaC2. The histopathology and isozyme assay were performed to analyze the changes in the activities of the genes affected by the free radicals released from CaC2. The molecular analysis included different isozymes namely esterase and acid phosphatase. Polyacrylamide electrophoresis of whole cell extract of control subjects and CaC2 administered rats were performed; subsequently the gels were treated with the substrates for acid phosphatase and esterase respectively. No difference was observed in the whole cell extract band pattern between the control subject and the CaC2 administered rats, which grossly indicates that the CaC2 has no effect on the expression pattern of isozymes (acid phosphatase and esterase). Histopathological analysis of liver, heart, spleen, kidney and lungs were performed to observe any change due to the administration of CaC2. Remarkable changes were observed during the histopathological study of lungs and kidney only. The histopathological analysis of kidney showed the thickening of the lining of collecting tubules with changes in cell structure while lungs were found to be increased moderately in weight, with focal areas of consolidation that was found red-brown to red. Key words: Calcium carbide; Histopathological study; Isozymes Dhaka Univ. J. Pharm. Sci. 6(2): 93-98, 2007 (December)

scholarly journals Visualizing the splicing of single pre-mRNA molecules in whole cell extract

RNA ◽  
2007 ◽  
Vol 14 (1) ◽  
pp. 170-179 ◽  
Author(s):  
D. J. Crawford ◽  
A. A. Hoskins ◽  
L. J. Friedman ◽  
J. Gelles ◽  
M. J. Moore
Keyword(s):  
Cell Extract ◽  
Whole Cell ◽  
Whole Cell Extract

scholarly journals V(D)J Recombination: Modulation of RAG1 and RAG2 Cleavage Activity on 12/23 Substrates by Whole Cell Extract and DNA-bending Proteins

1997 ◽  
Vol 185 (11) ◽  
pp. 2025-2032 ◽  
Author(s):  
Dennis J. Sawchuk ◽  
Frances Weis-Garcia ◽  
Sohail Malik ◽  
Eva Besmer ◽  
Michael Bustin ◽  
...  
Keyword(s):  
Dna Cleavage ◽  
Gene Rearrangement ◽  
Receptor Gene ◽  
Cell Extract ◽  
Base Pairs ◽  
Whole Cell ◽  
Recombination Activating Genes ◽  
Cleavage Activity ◽  
Recombination Signal Sequences ◽  
Whole Cell Extract

Antigen receptor gene rearrangement is directed by DNA motifs consisting of a conserved heptamer and nonamer separated by a nonconserved spacer of either 12 or 23 base pairs (12 or 23 recombination signal sequences [RSS]). V(D)J recombination requires that the rearranging DNA segments be flanked by RSSs of different spacer lengths, a phenomenon known as the 12/23 rule. Recent studies have shown that this restriction operates at the level of DNA cleavage, which is mediated by the products of the recombination activating genes RAG1 and RAG2. Here, we show that RAG1 and RAG2 are not sufficient for 12/23 dependent cleavage, whereas RAG1 and RAG2 complemented with whole cell extract faithfully recapitulates the 12/23 rule. In addition, HMG box containing proteins HMG1 and HMG2 enhance RAG1- and RAG2-mediated cleavage of substrates containing 23 RSS but not of substrates containing only 12 RSS. These results suggest the existence of a nucleoprotein complex at the cleavage site, consisting of architectural, catalytic, and regulatory components.

The Activation of Matrix Metalloproteinases by a Whole-cell Extract from Prevotella nigrescens

2009 ◽  
Vol 35 (1) ◽  
pp. 55-59 ◽  
Author(s):  
Takashi Itoh ◽  
Hiroshi Nakamura ◽  
Jun-ichi Kishi ◽  
Taro Hayakawa
Keyword(s):  
Matrix Metalloproteinases ◽  
Cell Extract ◽  
Whole Cell ◽  
Prevotella Nigrescens ◽  
Whole Cell Extract

scholarly journals DNA-dependent transcription of adenovirus genes in a soluble whole-cell extract.

1980 ◽  
Vol 77 (7) ◽  
pp. 3855-3859 ◽  
Author(s):  
J. L. Manley ◽  
A. Fire ◽  
A. Cano ◽  
P. A. Sharp ◽  
M. L. Gefter
Keyword(s):  
Cell Extract ◽  
Whole Cell ◽  
Whole Cell Extract

scholarly journals The ultrastructure and ATPase nature of polar membrane in Campylobacter jejuni

1988 ◽  
Vol 34 (5) ◽  
pp. 594-604 ◽  
Author(s):  
F. M. Brock ◽  
R. G. E. Murray
Keyword(s):  
Atpase Activity ◽  
Campylobacter Jejuni ◽  
Rat Liver ◽  
Liver Mitochondria ◽  
Cell Extract ◽  
Histochemical Staining ◽  
Soluble Form ◽  
Rat Liver Mitochondria ◽  
Whole Cell ◽  
Whole Cell Extract

Polar membrane in Campylobacter jejuni has been visualized on membrane vesicles. It was composed of doughnut-shaped particles 5–6 nm in diameter, with stalks, arranged in a hexagonal array. This structure was stabilized on the membrane by a high ionic strength buffer in the presence of 2-mercaptoethanol. Histochemical staining indicated localized ATPase activity at the poles of the cells. An ATPase with distinctive properties has been isolated and purified from this organism; it gives a specific activity of approximately 0.3 units/mg of protein. Electron microscopy showed doughnut-shaped particles 5–6 nm in diameter. Nondissociating and sodium dodecyl sulfate – polyacrylamide gel electrophoresis of the purified enzyme revealed, respectively, a single band with ATPase activity and a molecular weight of ca. 75 – 000 Da. The enzyme was cold labile and activity was abolished by trypsin. Dicylohexylcarbodiimide inhibited the membranebound form of the enzyme, but did not inhibit the soluble form. Oligomycin had no inhibitory activity on either form of the enzyme. The enzyme specifically hydrolysed ATP, but other nucleotide substrates were not degraded. The enzyme was activated by Mg2+ and inhibited by Ca2+, whereas other ions had no effect on activity. Antibodies prepared to this enzyme bound to the polar regions of whole cells as shown by protein A – colloidal gold immunoelectron microscopy. The antibodies to this ATPase cross reacted (shown by Western blotting) with four proteins from a whole-cell extract of this organism, two proteins in Aquaspirillum serpens MW5, and three proteins from Escherichia coli K12. They did not cross-react with any proteins from Spirillum volutans, Methanococcus voltae, Vibrio cholerae, or rat liver mitochondria. Antibodies raised against the F1-ATPase of E. coli K12 cross reacted with six proteins in a whole-cell extract of this organism, and one protein species in each of the whole-cell extracts of V. cholera, A. serpens MW5, S. volutans, and rat liver mitochondria. These antibodies did not recognize any whole cell proteins from either C. jejuni or M. voltae. These results along with the ATPase activity localized by histochemical staining suggest that polar membrane is an assembly of ATPase molecules at the poles of the cell and that the ATPase isolated from C. jejuni is serologically and structurally unusual.

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