Further evidence for hyaluronidase activity of Treponema pallidum

1983 ◽  
Vol 29 (11) ◽  
pp. 1507-1513 ◽  
Author(s):  
T. J. Fitzgerald ◽  
E. M. Gannon
Keyword(s):  
Enzyme Activity ◽  
Hyaluronic Acid ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Capillary Permeability ◽  
Treponema Pallidum ◽  
Intradermal Injection ◽  
Hyaluronidase Activity ◽  
Immunologic Reactions

The presence of hyaluronidase in preparations of Treponema pallidum was previously shown using acidified bovine serum albumin reactions and Ouchterlony immunodiffusion. To expand on these preliminary findings more sensitive techniques of viscometry, additional immunologic reactions, and altered capillary permeability were used to characterize treponemal-associated hyaluronidase. The pathogens T. pallidum and T. pertenue degraded hyaluronic acid, whereas the nonpathogens T. denticola and T. vincentii did not. As syphilitic infection progressed, hyaluronidase activity decreased; organisms harvested from 14-day testicular infections degraded hyaluronic acid less rapidly than organisms from 4-day infections. Uninfected rabbit testicular extract also exhibited significant enzyme activity. The neutralizing activity of immune sera was decreased by prior adsorption with bovine hyaluronidase, suggesting that some of the neutralizing factors are associated with this enzyme. Radioimmunoassay was used to quantitate antibodies to hyaluronidase in immune sera. Antihyaluronidase sera were isolated from rabbits immunized with bovine hyaluronidase. Treponema pallidum, as well as uninfected rabbit testicular extract, cross-reacted with these antisera. Immunofluorescence indicated that the hyaluronidase was uniformly distributed along the treponemal surface. As a final indicator of hyaluronidase activity, alterations in capillary permeability were detected 1 h after intradermal injection of T. pallidum.

scholarly journals Enzyme Stability in Nanoparticle Preparations Part 1: Bovine Serum Albumin Improves Enzyme Function

Molecules ◽  
2020 ◽  
Vol 25 (20) ◽  
pp. 4593
Author(s):  
Jason Thomas Duskey ◽  
Federica da Ros ◽  
Ilaria Ottonelli ◽  
Barbara Zambelli ◽  
Maria Angela Vandelli ◽  
...  
Keyword(s):  
Enzyme Activity ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Specific Activity ◽  
Enzyme Stability ◽  
Polymeric Nanoparticles ◽  
Release Kinetics ◽  
Titration Calorimetry ◽  
Therapeutic Effects

Enzymes have gained attention for their role in numerous disease states, calling for research for their efficient delivery. Loading enzymes into polymeric nanoparticles to improve biodistribution, stability, and targeting in vivo has led the field with promising results, but these enzymes still suffer from a degradation effect during the formulation process that leads to lower kinetics and specific activity leading to a loss of therapeutic potential. Stabilizers, such as bovine serum albumin (BSA), can be beneficial, but the knowledge and understanding of their interaction with enzymes are not fully elucidated. To this end, the interaction of BSA with a model enzyme B-Glu, part of the hydrolase class and linked to Gaucher disease, was analyzed. To quantify the natural interaction of beta-glucosidase (B-Glu,) and BSA in solution, isothermal titration calorimetry (ITC) analysis was performed. Afterwards, polymeric nanoparticles encapsulating these complexes were fully characterized, and the encapsulation efficiency, activity of the encapsulated enzyme, and release kinetics of the enzyme were compared. ITC results showed that a natural binding of 1:1 was seen between B-Glu and BSA. Complex concentrations did not affect nanoparticle characteristics which maintained a size between 250 and 350 nm, but increased loading capacity (from 6% to 30%), enzyme activity, and extended-release kinetics (from less than one day to six days) were observed for particles containing higher B-Glu:BSA ratios. These results highlight the importance of understanding enzyme:stabilizer interactions in various nanoparticle systems to improve not only enzyme activity but also biodistribution and release kinetics for improved therapeutic effects. These results will be critical to fully characterize and compare the effect of stabilizers, such as BSA with other, more relevant therapeutic enzymes for central nervous system (CNS) disease treatments.

Bovine serum albumin gel/polyelectrolyte complex of hyaluronic acid and chitosan based microcarriers for Sorafenib targeted delivery

2020 ◽  
Vol 137 (34) ◽  
pp. 49002 ◽  
Author(s):  
Violeta Paşcalău ◽  
Mihaela Tertis ◽  
Emoke Pall ◽  
Maria Suciu ◽  
Traian Marinca ◽  
...  
Keyword(s):  
Hyaluronic Acid ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Targeted Delivery ◽  
Bovine Serum ◽  
Polyelectrolyte Complex

The hyaluronan–protein complexes at low ionic strength: How the hyaluronidase activity is controlled by the bovine serum albumin

2009 ◽  
Vol 28 (6) ◽  
pp. 365-372 ◽  
Author(s):  
Hélène Lenormand ◽  
Frédéric Tranchepain ◽  
Brigitte Deschrevel ◽  
Jean-Claude Vincent
Keyword(s):  
Ionic Strength ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Protein Complexes ◽  
Hyaluronidase Activity ◽  
Low Ionic Strength

Improvement of an artificial test substrate technique for evaluation of em immunocytochemical labeling

1987 ◽  
Vol 45 ◽  
pp. 762-763
Author(s):  
G. D. Gagne ◽  
M. F. Miller
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Artificial Substrate ◽  
Chemical Fixation ◽  
As If

We recently described an artificial substrate system which could be used to optimize labeling parameters in EM immunocytochemistry (ICC). The system utilizes blocks of glutaraldehyde polymerized bovine serum albumin (BSA) into which an antigen is incorporated by a soaking procedure. The resulting antigen impregnated blocks can then be fixed and embedded as if they are pieces of tissue and the effects of fixation, embedding and other parameters on the ability of incorporated antigen to be immunocyto-chemically labeled can then be assessed. In developing this system further, we discovered that the BSA substrate can also be dried and then sectioned for immunolabeling with or without prior chemical fixation and without exposing the antigen to embedding reagents. The effects of fixation and embedding protocols can thus be evaluated separately.

Stability of Prostacyclin in Human Plasma and Whole Blood: Studies on the Protective Effect of Albumin

1981 ◽  
Vol 46 (03) ◽  
pp. 645-647 ◽  
Author(s):  
M A Orchard ◽  
C Robinson
Keyword(s):  
Platelet Aggregation ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Protective Effect ◽  
Whole Blood ◽  
Bovine Serum ◽  
Fatty Acid Content ◽  
Krebs Solution ◽  
Antiaggregatory Activity ◽  
Free Plasma

SummaryThe biological half-life of prostacyclin in Krebs solution, human cell-free plasma or whole blood was measured by bracket assay on ADP-induced platelet aggregation. At 37°C, pH 7.4, plasma and blood reduced the rate of loss of antiaggregatory activity compared with Krebs solution. The protective effect of plasma was greater than that of whole blood. This effect could be partially mimicked by the addition of human or bovine serum albumin to the Krebs solution. The stabilisation afforded by human serum albumin was dependent on the fatty acid content of the albumin, although this was less important for bovine serum albumin.

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