Immobilization of Aprotinin to Fibrinogen as a Novel Method for Controlling Degradation of Fibrin Gels

2007 ◽  
Vol 18 (3) ◽  
pp. 695-701 ◽  
Author(s):  
Jason D. Smith ◽  
Andrew Chen ◽  
Lauren A. Ernst ◽  
Alan S. Waggoner ◽  
Phil G. Campbell
Keyword(s):  
Fibrin Gels ◽  
Novel Method

The removal and morphology of intact biofilms from implanted venous access devices

1995 ◽  
Vol 53 ◽  
pp. 1020-1021
Author(s):  
M.A. Gregory ◽  
G.P. Hadley
Keyword(s):  
Patient Selection ◽  
Surgical Oncology ◽  
Venous Access ◽  
Common Procedure ◽  
Indwelling Catheters ◽  
Careful Patient ◽  
Novel Method ◽  
The Subject ◽  
Vascular Catheters ◽  
Venous Access Devices

The insertion of implanted venous access systems for children undergoing prolonged courses of chemotherapy has become a common procedure in pediatric surgical oncology. While not permanently implanted, the devices are expected to remain functional until cure of the primary disease is assured. Despite careful patient selection and standardised insertion and access techniques, some devices fail. The most commonly encountered problems are colonisation of the device with bacteria and catheter occlusion. Both of these difficulties relate to the development of a biofilm within the port and catheter. The morphology and evolution of biofilms in indwelling vascular catheters is the subject of ongoing investigation. To date, however, such investigations have been confined to the examination of fragments of biofilm scraped or sonicated from sections of catheter. This report describes a novel method for the extraction of intact biofilms from indwelling catheters.15 children with Wilm’s tumour and who had received venous implants were studied. Catheters were removed because of infection (n=6) or electively at the end of chemotherapy.

Longitudinal Changes in Individual BrainAGE in Healthy Aging, Mild Cognitive Impairment, and Alzheimer’s Disease

GeroPsych ◽  
2012 ◽  
Vol 25 (4) ◽  
pp. 235-245 ◽  
Author(s):  
Katja Franke ◽  
Christian Gaser
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Healthy Aging ◽  
Brain Aging ◽  
Elderly Subjects ◽  
Additional Increase ◽  
Longitudinal Changes ◽  
Novel Method ◽  
The Brain

We recently proposed a novel method that aggregates the multidimensional aging pattern across the brain to a single value. This method proved to provide stable and reliable estimates of brain aging – even across different scanners. While investigating longitudinal changes in BrainAGE in about 400 elderly subjects, we discovered that patients with Alzheimer’s disease and subjects who had converted to AD within 3 years showed accelerated brain atrophy by +6 years at baseline. An additional increase in BrainAGE accumulated to a score of about +9 years during follow-up. Accelerated brain aging was related to prospective cognitive decline and disease severity. In conclusion, the BrainAGE framework indicates discrepancies in brain aging and could thus serve as an indicator for cognitive functioning in the future.

Novel method of mitral annular enlargement for implantation of an oversized mitral valve prosthesis

2014 ◽  
Vol 62 (S 02) ◽  
Author(s):  
J. Photiadis ◽  
M. Musci ◽  
O. Miera ◽  
S. Ovroutski ◽  
A. Mekkawy ◽  
...  
Keyword(s):  
Mitral Valve ◽  
Valve Prosthesis ◽  
Mitral Valve Prosthesis ◽  
Novel Method

Effect of Glycosaminoglycans on Thrombin- and Atroxin-Induced Fibrin Assembly and Structure

1989 ◽  
Vol 62 (04) ◽  
pp. 1057-1061 ◽  
Author(s):  
Marcus E Carr ◽  
Patrick L Powers
Keyword(s):  
Chondroitin Sulfate ◽  
Fiber Diameter ◽  
Lag Phase ◽  
Low Molecular Weight ◽  
Fibrin Gels ◽  
Fiber Size ◽  
Induced Changes ◽  
The Impact ◽  
Fiber Radius ◽  
Turbidity Increase

SummaryThis study was performed to quantitate the impact of several glycosaminoglycans (GAG) on fibrin assembly and structure. Gel formation was monitored as the increase in optical density at 633 nm subsequent to thrombin (2 NIH u/ml) or atroxin (0.10 mg/ml) addition to solutions of buffered fibrinogen (1 mg/ml) or plasma. Gel absorbance was measured as a function of wavelength (400 to 800 nm) and gel fiber diameter and mass/length ratio (μ) were calculated. Chondroitin sulfate A (CSA)shortened the lag phase, enhanced the maximal rate of turbidity increase, and increased the final gel turbidity of fibrin gels formed by thrombin or atroxin. CSA (16 mg/ml) increased fiber μ from 1.3 to 3.1 × 1013 dalton/cm and fiber radius from 6.0 to 8.6 × 10-6 cm in thrombin-induced gels. μ increased from 0.7 to 2.7 × 1013 dalton/cm and fiber radius from 4 to 7.8 × 10-6 cm for atroxin-induced gels. Above 16 mg/ml, CSA caused fibrinogen precipitation in purified solutions but not in plasma. CSA inhibited thrombin-induced plasma clotting of plasma but effects in atroxin-mediated plasma gels paralleled those seen in purified solutions. Chondroitin sulfate B (CSB)-induced changes in fibrin were similar but slightly less dramatic than those seen with CSA. μ increased from 0.9 to 2.0 × 1013 dalton/cm for thrombin-induced fibrin gels and from 0.8 to 2.3 × 1013 dalton/cm for atroxininduced gels. Low molecular weight heparin (Mr = 5100) slowed fibrin assembly and reduced fiber size by 50% in thrombininduced gels. Changes in μ of atroxin-induced gels were much less pronounced (<20%). This study documents pronounced GAGinduced changes in fibrin structure which vary with GAG species and may mediate significant physiologic functions.

A Novel Method for the Rapid Purification of Human and Rat Fibrin(OGEN) Degradation Products in High Yields

1979 ◽  
Author(s):  
W. Nieuwenhuizen ◽  
I. A. M. van Ruijven-Vermeer ◽  
F. Haverkate ◽  
G. Timan
Keyword(s):  
Degradation Products ◽  
Complete Separation ◽  
Purification Method ◽  
Amino Terminal ◽  
Novel Method ◽  
Rapid Purification ◽  
The One ◽  
High Yields ◽  
Size Heterogeneity ◽  
D Dimer

A novel method will be described for the preparation and purification of fibrin(ogen) degradation products in high yields. The high yields are due to two factors. on the one hand an improved preparation method in which the size heterogeneity of the degradation products D is strongly reduced by plasmin digestion at well-controlled calcium concentrations. At calcium concentrations of 2mM exclusively D fragments, M.W.= 93-000 (Dcate) were formed; in the presence of 1OmM EGTA only fragments M.W.= 80.000 (D EGTA) were formed as described. on the other hand a new purification method, which includes Sephadex G-200 filtration to purify the D:E complexes and separation of the D and E fragments by a 16 hrs. preparative isoelectric focussing. The latter step gives a complete separation of D (fragments) (pH = 6.5) and E fragments (at pH = 4.5) without any overlap, thus allowing a nearly 100% recovery in this step. The overall recoveries are around 75% of the theoretical values. These recoveries are superior to those of existing procedures. Moreover the conditions of this purification procedure are very mild and probably do not affect the native configuration of the products. Amino-terminal amino acids of human Dcate, D EGTA and D-dimer are identical i.e. val, asx and ser. in the ratgly, asx and ser were found. E 1% for rat Dcate=17-8 for rat D EGTA=16.2 and for rat D- dimer=l8.3. for the corresponding human fragments, these values were all 20.0 ± 0.2.

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