scholarly journals Mode of aggregation of hyaluronic acid protein complex on the surface of articular cartilage.

1970 ◽  
Vol 29 (6) ◽  
pp. 591-602 ◽  
Author(s):  
P S Walker ◽  
A Unsworth ◽  
D Dowson ◽  
J Sikorski ◽  
V Wright
Keyword(s):  
Hyaluronic Acid ◽  
Articular Cartilage ◽  
Protein Complex ◽  
Acid Protein

Fingerprinting the hyaluronic acid-protein complex of human vitreous humour

1965 ◽  
Vol 11 (2) ◽  
pp. 139-145 ◽  
Author(s):  
S.A. Barker ◽  
S.J. Crews ◽  
J.B. Marsters ◽  
M. Stacey
Keyword(s):  
Hyaluronic Acid ◽  
Protein Complex ◽  
Vitreous Humour ◽  
Acid Protein

scholarly journals The diffusion coefficient of caffeine through agar gels containing a hyaluronic acid–protein complex. A model system for the study of the permeability of connective tissues

1972 ◽  
Vol 127 (1) ◽  
pp. 249-253 ◽  
Author(s):  
M. McCabe
Keyword(s):  
Diffusion Coefficient ◽  
Hyaluronic Acid ◽  
Protein Complex ◽  
Model System ◽  
Large Decrease ◽  
Connective Tissues ◽  
Agar Gel ◽  
Acid Protein ◽  
Agar Gels ◽  
Physicochemical Measurements

A hyaluronic acid–protein complex was embedded into agar gel. This gel complex resembles in some respects the physiological situation in connective tissue, but still permits precise physicochemical measurements to be made. The diffusion coefficient of caffeine into and from such gels has been measured as a function of both agar and hyaluronate concentration. The value for the diffusion coefficient of caffeine was also measured by using a Gouy type diffusiometer. From both types of measurement the value for D (Fick) for caffeine when extrapolated to zero caffeine and agar concentrations agreed at (6.79±0.01)×10−6cm2·s−1 at 25°C. Although agar concentration had only a small effect on caffeine diffusion, hyaluronic acid caused a large decrease in caffeine diffusion co-efficient. The presence of the hyaluronic acid–protein complex within the gel tended to oppose gel syneresis, a concentration of 1.7mg/ml abolishing the effect and higher concentrations reversing it. The possible physiological implications of these results are discussed.

scholarly journals AN INVESTIGATION OF THE FOLIC ACID-PROTEIN COMPLEX IN YEAST

1950 ◽  
Vol 182 (1) ◽  
pp. 367-384
Author(s):  
V.G. Allfrey ◽  
C.G. King
Keyword(s):  
Folic Acid ◽  
Protein Complex ◽  
Acid Protein

Analysis of the effect of cationic hyaluronic acid on articular cartilage

2021 ◽  
Vol 29 ◽  
pp. S116-S117
Author(s):  
Y. Kamada ◽  
H. Inoue ◽  
S. Nakagawa ◽  
Y. Fujii ◽  
K. Kaihara ◽  
...  
Keyword(s):  
Hyaluronic Acid ◽  
Articular Cartilage

5S Ribonucleic acid-protein complex extracted from rat liver ribosomes by formamide

Biochemistry ◽  
1972 ◽  
Vol 11 (12) ◽  
pp. 2323-2326 ◽  
Author(s):  
Mary L. Petermann ◽  
Mary G. Hamilton ◽  
Amalia Pavlovec
Keyword(s):  
Rat Liver ◽  
Protein Complex ◽  
Ribonucleic Acid ◽  
Acid Protein ◽  
Liver Ribosomes

scholarly journals The properties of proteoglycan prepared from human articular cartilage by using associative caesium chloride gradients of high and low starting densities

1985 ◽  
Vol 232 (1) ◽  
pp. 111-117 ◽  
Author(s):  
M T Bayliss ◽  
P J Roughley
Keyword(s):  
Hyaluronic Acid ◽  
Articular Cartilage ◽  
Proteinase Inhibitors ◽  
Density Gradient Centrifugation ◽  
Gradient Centrifugation ◽  
Human Articular Cartilage ◽  
Adult Human ◽  
Cscl Density Gradient ◽  
Proteoglycan Aggregates ◽  
Hyaluronic Acid Binding

Proteoglycan was extracted from adult human articular cartilage from both the knee and the hip, and A1 preparations were prepared by CsCl-density-gradient centrifugation at starting densities of 1.69 and 1.5 g/ml. Irrespective of whether the cartilage was diced to 1 mm cubes or sectioned to 20 micron slices there was always a lower proportion of both protein and proteoglycan aggregate in the A1 preparation prepared at 1.69 g/ml. Furthermore, the addition of exogenous hyaluronic acid to the extracts before centrifugation did not improve the yield of aggregate at 1.69 g/ml. These results were not affected by the presence of proteinase inhibitors in the extraction medium. It appears that adult human articular cartilage contains a high proportion of low-density proteoglycan subunits and hyaluronic acid-binding proteins that make most of the re-formed proteoglycan aggregates of a lower density than is usually encountered with younger human and mammalian hyaline cartilages.

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