Comparisons of rotavirus polypeptides by limited proteolysis: close similarity of certain polypeptides of different strains.

1981 ◽  
Vol 40 (3) ◽  
pp. 720-728 ◽  
Author(s):  
M L Dyall-Smith ◽  
I H Holmes
Keyword(s):  
Limited Proteolysis ◽  
Close Similarity ◽  
Different Strains

Ultrastructural Changes of the Symbiotic Chlorella-Like Alga Isolated from Hydra Viridis

1982 ◽  
Vol 40 ◽  
pp. 320-321
Author(s):  
K.W. Lee ◽  
R.H. Meints ◽  
D. Kuczmarski ◽  
J.L. Van Etten
Keyword(s):  
Time Course ◽  
Reciprocal Cross ◽  
Ultrastructural Level ◽  
Ultrastructural Changes ◽  
Symbiotic Relationship ◽  
Cell Recognition ◽  
Green Hydra ◽  
Different Strains ◽  
Hydra Viridis

The physiological, biochemical, and ultrastructural aspects of the symbiotic relationship between the Chlorella-like algae and the hydra have been intensively investigated. Reciprocal cross-transfer of the Chlorellalike algae between different strains of green hydra provide a system for the study of cell recognition. However, our attempts to culture the algae free of the host hydra of the Florida strain, Hydra viridis, have been consistently unsuccessful. We were, therefore, prompted to examine the isolated algae at the ultrastructural level on a time course.

Limited Proteolysis of Vitronectin by Plasmin Destroys Heparin Binding Activity

1991 ◽  
Vol 66 (03) ◽  
pp. 310-314 ◽  
Author(s):  
David C Sane ◽  
Tammy L Moser ◽  
Charles S Greenberg
Keyword(s):  
Limited Proteolysis ◽  
Plasminogen Activator Inhibitor ◽  
Binding Activity ◽  
Binding Domain ◽  
Heparin Binding ◽  
Inhibitor Type ◽  
Activator Inhibitor Type ◽  
Activator Inhibitor ◽  
Pai 1

SummaryVitronectin (VN) stabilizes plasminogen activator inhibitor type 1 (PAI-1) activity and prevents the fibrin(ogen)-induced acceleration of plasminogen activation by t-PA. These antifibrinolytic activities as well as other functions are mediated by the glycosaminoglycan (GAG) binding domain of VN. Since the GAG binding region is rich in arginyl and lysyl residues, it is a potential target for enzymes such as plasmin. In this paper, the dose and time-dependent proteolysis of VN by plasmin is demonstrated. The addition of urokinase or streptokinase (200 units/ml) to plasma also produced proteolysis of VN. With minimal proteolysis, the 75 kDa band was degraded to a 62-65 kDa form of VN. This minimal proteolysis destroyed the binding of [3H]-heparin to VN and reversed the neutralization of heparin by VN.Thus, the plasmin-mediated proteolysis of the GAG binding activity of VN could destroy the antifibrinolytic activity of VN during physiologic conditions and during thrombolytic therapy. Furthermore, other functions of VN in complement and coagulation systems that are mediated by the GAG binding domain may be destroyed by plasmin proteolysis.

A Sensitive and Facile Assay for the Measurement of Activated Protein C Activity Levels in Vivo

1993 ◽  
Vol 69 (05) ◽  
pp. 441-447 ◽  
Author(s):  
Carolyn L Orthner ◽  
Billy Kolen ◽  
William N Drohan
Keyword(s):  
Protein C ◽  
Plasma Concentrations ◽  
Limited Proteolysis ◽  
Activated Protein C ◽  
Microtiter Plate ◽  
Reversible Inhibitor ◽  
Activity Levels ◽  
Standard Curve ◽  
Agarose Beads

SummaryActivated protein C (APC) is a serine protease which plays an important role as a naturally occurring antithrombotic enzyme. APC, which is formed by thrombin-catalyzed limited proteolysis of the zymogen protein C, functions as an anticoagulant by proteolytic inactivation of the coagulation cofactors VIIIa and Va. APC is inhibited by several members of the serpin family as well a by α2-macroglobulin. APC is being developed as a therapeutic for the prevention and treatment of thrombosis. We have developed an assay to quantify circulating levels of enzymatically active APC during its administration to patients, in healthy individuals, and in various disease states. This assay utilizes an EDTA-dependent anti-protein C monoclonal antibody (Mab) 7D7B10 to capture both APC and protein C from plasma, prepared from blood collected in an anticoagulant supplemented with the reversible inhibitor p-aminobenzamidine. Mab 7D7B10-derivatized agarose beads are added to the wells of a 96-well filtration plate, equilibrated with Tris-buffered saline, and incubated for 10 min with 200 μl of plasma. After washing, APC and protein C are eluted from the immunosorbent beads with a calcium-containing buffer into the wells of a 96-well microtiter plate containing antithrombin III (ATIII) and heparin. The amidolytic activity of APC is then measured on a kinetic plate reader following the addition of L-pyroglutamyl-L-prolyl-L-arginine-p-nitroanilide (S-2366) substrate.The rate of substrate hydrolysis was proportional to APC concentration over a 200-fold concentration range (5.0 to 1,000 ng/ml) when measured continuously over a 15 to 30 min time period. The coefficient of variation was 5.9% at 35 ng/ml and 8.8% at 350 ng/ml APC. The sensitivity of the assay could be increased by measuring the amount of color produced after longer incubation times in the endpoint mode. The measured APC activity levels were little affected by varying protein C or prothrombin over the extremes of 0 to 150% of normal plasma concentrations. By constructing the standard curve in protein C-deficient plasma, the concentration of APC activity in normal pooled plasma was determined to be 2.8 ng/ml (45 pM), which represents 0.08% of the protein C concentration. The assay was approximately 50-fold more sensitive than the identical assay, but using Mab-coated microtiter wells rather than immunosorbent beads as the capture step.

HS-SPME/GC-MS Assisted Analysis of Volatile Constituents in Different Strains of Shiitake Culinary- Medicinal Mushroom, Lentinus edodes (Agaricomycetes)

2019 ◽  
Vol 21 (7) ◽  
pp. 693-702
Author(s):  
Lívia Martinez Abreu Soares Costa ◽  
Maiara Andrade de Carvalho Sousa ◽  
Thiago Pereira Souza ◽  
Whasley Ferreira Duarte ◽  
Diego Cunha Zied ◽  
...  
Keyword(s):  
Medicinal Mushroom ◽  
Lentinus Edodes ◽  
Volatile Constituents ◽  
Different Strains ◽  
Assisted Analysis

Antioxidant and Antibacterial Activities of Artemisia herba-alba Asso Essential Oil from Middle Atlas, Morocco

2018 ◽  
Vol 16 (S1) ◽  
pp. S48-S54
Author(s):  
Y. Ez zoubi ◽  
S. Lairini ◽  
A. Farah ◽  
K. Taghzouti ◽  
A. El Ouali Lalami
Keyword(s):  
Antibacterial Activity ◽  
Essential Oil ◽  
Foodborne Pathogens ◽  
Food Systems ◽  
Antibacterial Activities ◽  
Culture Collection ◽  
Bornyl Acetate ◽  
Bacterial Strains ◽  
Disk Diffusion Assay ◽  
Different Strains

The purpose of this study was to determine the chemical composition and to evaluate the antioxidant and antibacterial effects of the Moroccan Artemisia herba-alba Asso essential oil against foodborne pathogens. The essential oil of Artemisia herba-alba was analyzed by gas chromatography coupled with mass spectroscopy. The antibacterial activity was assessed against three bacterial strains isolated from foodstuff and three bacterial strains referenced by the ATCC (American Type Culture Collection) using the disk diffusion assay and the macrodilution method. The antioxidant activity was evaluated using the DPPH (2, 2-diphenyl-1- picrylhydrazyl) method. The fourteen compounds of the Artemisia herba-alba essential oil were identified; the main components were identified as β-thujone, chrysanthenone, α-terpineol, α-thujone, α-pinene, and bornyl acetate. The results of the antibacterial activity obtained showed a sensitivity of the different strains to Artemisia herba-alba essential oil with an inhibition diameter of 8.50 to 17.00 mm. Concerning the MICs (minimum inhibitory concentrations), the essential oil exhibited much higher antibacterial activity with MIC values of 2.5 μl/ml against Bacillus subtilis ATCC and Lactobacillus sp. The essential oil was found to be active by inhibiting free radicals with an IC50 (concentration of an inhibitor where the response is reduced by half) value of 2.9 μg/ml. These results indicate the possible use of the essential oil on food systems as an effective inhibitor of foodborne pathogens, as a natural antioxidant, and for potential pharmaceutical applications. However, further research is needed in order to determine the toxicity, antibacterial, and antioxidant effects in edible products.

Memroses Motif Jumputan di Atas Keramik

2019 ◽  
Vol 6 (1) ◽  
Author(s):  
Tri Wahyuni
Keyword(s):  
Close Similarity ◽  
Visual Effect ◽  
Cobalt Blue

AbstrakKarya ini sebenarnya adalah sebuah eksperimen, sebuah eksplorasi atas kemungkinan-kemungkinan penerapan motif jumputanbiru pada permukaan keramik. Proses ini bagaimana sebuah penjelajahan tanpa akhir yang hasil-hasilnya menawarkan secaravisual ruang untuk berimajinasi yang selalu penuh dengan kejutan yang dihasilkan dari ikatan, lipatan, kerutan, jelujur, danpewarnaan. Warna dan motif pada kain shibori biru dan pada keramik warna biru cobalt memiliki persamaa yang dekat dalamhal warna. Kesamaan ini dipandang sebagai representasi shibori biru yang diterapkan pada tekstil. Efek visual memunculkanspirit jumputan biru pada keramik yang tidak lagi mengacu pada pemaknaan yang ada pada kain jumputan biru.AbstractThe work I have completed is basically an experiment, an exploration of the possibilities applying blue shibori motif on ceramicsurface. This process is like a never-ending exploration of which the results visually offer space to have imaginations, alwaysfull of surprises resulting from the process of knotting, folding, wrinkling, stitching and coloring. The color and motif on blueshibori cloth and on cobalt blue ceramic have close similarity in color. This similarity is regarded as the representation of blueshibori as applied on textile. The visual effect of this process brings out the spirit of blue shibori on ceramic, which does notrefer to the meaning existing in the blue shibori cloth.

Transport of escherichia coli through soil to groundwater traced by randomly amplified polymorphic DNA (RAPD)

1997 ◽  
Vol 35 (11-12) ◽  
pp. 351-357 ◽  
Author(s):  
R. Rothmaier ◽  
A. Weidenmann ◽  
K. Botzenhart
Keyword(s):  
Negative Impact ◽  
Random Amplified Polymorphic Dna ◽  
Coli Strain ◽  
Soil Samples ◽  
Test Field ◽  
Liquid Manure ◽  
E Coli ◽  
Rapd Pattern ◽  
Geological Situation ◽  
Different Strains

Isolates (50) of E. coli obtained from liquid manure (20 bovine, 20 porcine) were genotyped using random amplified polymorphic DNA (RAPD). Typing revealed 9 and 14 different strains in bovine and porcine liquid manure respectively with no strains in common. One porcine strain, showing a simple RAPD pattern, was subcultured and spread on a test field (1.5l/m2 at 1010 cfu/l) in a drinking water protection zone with loamy to sandy sediments in the Donauried area, Baden-Wurttemberg. Soil samples and groundwaters were collected at monthly intervals October 1994 – June 1995 during which 114 E. coli isolates were recovered. The first occurrence and maximum concentration of E. coli in soil samples taken from more than 20cm depth was in January 1995, declining rapidly with depth and time. All isolates from soil and only one from groundwater showed the RAPD pattern of the spread E. coli strain. The results could not demonstrate a severe negative impact of the spreading of liquid manure on the bacteriological quality of the groundwater in the given geological situation. The distinct strain patterns found in different kinds of liquid manure suggest that genotyping of E. coli by RAPD may be an adequate tool for tracing sources of faecal contamination.

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