Electrostatic Interactions in Docking a 3D Model of Bovine Testicular Hyaluronidase with a Chondroitin Sulfate Trimer and a Heparin Tetramer

2018 ◽  
Vol 73 (5) ◽  
pp. 223-230
Author(s):  
A. V. Maksimenko ◽  
R. S. Beabealashvili
1954 ◽  
Vol 37 (3) ◽  
pp. 361-371 ◽  
Author(s):  
E. W. Emmart ◽  
J. B. Longley

1. Following heat denaturation after an hour at boiling temperature bovine testicular hyaluronidase has been shown to undergo spontaneous reactivation. 2. This reactivation is a function of the temperature at which the enzyme solution is maintained. 3. Secondary inactivation was observed to follow a reactivation of the enzyme at all concentrations observed. 4. There is a relationship between hydrolysis by the enzyme and the purity of the substrate. The demonstration of activity of the freshly boiled enzyme by the turbidimetric reduction technique is dependent upon the purity of the substrate. 5. These reactions have been demonstrated using preparations of bovine and avian hyaluronic acid and porcine chondroitin sulfate.


Author(s):  
H. Clarke Anderson ◽  
Priscilla R. Coulter

Epiphyseal cartilage matrix contains fibrils and particles of at least 5 different types: 1. Banded collagen fibrils, present throughout the matrix, but not seen in the lacunae. 2. Non-periodic fine fibrils <100Å in diameter (Fig. 1), which are most notable in the lacunae, and may represent immature collagen. 3. Electron dense matrix granules (Fig. 1) which are often attached to fine fibrils and collagen fibrils, and probably contain protein-polysaccharide although the possibility of a mineral content has not been excluded. 4. Matrix vesicles (Fig. 2) which show a selective distribution throughout the epiphysis, and may play a role in calcification. 5. Needle-like apatite crystals (Fig. 2).Blocks of formalin-fixed epiphysis from weanling mice were digested with the following agents in 0.1M phosphate buffer: a) 5% ethylenediaminetetraacetate (EDTA) at pH 8.3, b) 0.015% bovine testicular hyaluronidase (Sigma, type IV, 750 units/mg) at pH 5.5, and c) 0.1% collagenase (Worthington, chromatograhically pure, 200 units/mg) at pH 7.4. All digestions were carried out at 37°C overnight. Following digestion tissues were examined by light and electron microscopy to determine changes in the various fibrils and particles of the matrix.


1979 ◽  
Vol 7 (6) ◽  
pp. 1287-1289 ◽  
Author(s):  
PETER GACESA ◽  
MARC J. SAVITSKY ◽  
KENNETH S. DODGSON ◽  
ANTHONY H. OLAVESEN

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