scholarly journals Isolation and properties of hyaluronic acid from bovine heart valves

1969 ◽  
Vol 113 (3) ◽  
pp. 559-563 ◽  
Author(s):  
F. A. Meyer ◽  
B. N. Preston ◽  
D. A. Lowther
Keyword(s):  
Hyaluronic Acid ◽  
Synovial Fluid ◽  
Heart Valves ◽  
Glucuronic Acid ◽  
Molecular Size ◽  
Sedimentation Equilibrium ◽  
Molar Ratio ◽  
Soluble Extract ◽  
Caesium Chloride ◽  
Bovine Heart

1. A soluble extract of bovine heart valves was obtained after the tissue had been pulverized at liquid-nitrogen temperatures in a mill. 2. Hyaluronic acid was isolated from the crude extract by sedimentation equilibrium in a caesium chloride density gradient (Franek & Dunstone, 1966). 3. Analysis of the product indicated that it contained 15% of protein and the molar ratio of glucuronic acid to glucosamine was 1·27. 4. Its physicochemical properties, as determined by lightscattering, viscosity and sedimentation studies, suggested that its molecular size and configuration were similar to those of hyaluronic acid isolated from ox synovial fluid (Preston, Davies & Ogston, 1965).

scholarly journals Isolation and properties of chondroitin sulphates from bovine heart valves

1970 ◽  
Vol 118 (4) ◽  
pp. 595-601 ◽  
Author(s):  
D. A. Lowther ◽  
B. N. Preston ◽  
F. A. Meyer
Keyword(s):  
Heart Valves ◽  
Chondroitin Sulphate ◽  
Sedimentation Equilibrium ◽  
Structural Studies ◽  
Variable Size ◽  
Keratan Sulphate ◽  
Molecular Weights ◽  
Caesium Chloride ◽  
Bovine Heart ◽  
Basic Model

1. Several protein–polysaccharides were isolated from the soluble extracts of bovine heart valves by sedimentation equilibrium in a caesium chloride density gradient (Meyer, Preston & Lowther, 1969). 2. Compositional and structural studies indicated that the polysaccharide moiety was chondroitin sulphate. Differences in the protein content of the products were observed. There was no evidence suggesting the presence of keratan sulphate. 3. Sedimentation studies indicated that the molecular weights of the samples were between 4.2×104 and 6.5×104. The results are discussed in terms of a basic model for the protein–polysaccharides of two polysaccharide chains linked by a protein of variable size.

scholarly journals The isolation and partial characterization of the major glycoprotein (LGP-I) from the articular lubricating fraction from bovine synovial fluid

1977 ◽  
Vol 161 (3) ◽  
pp. 473-485 ◽  
Author(s):  
D A Swann ◽  
S Sotman ◽  
M Dixon ◽  
C Brooks
Keyword(s):  
Amino Acids ◽  
Synovial Fluid ◽  
Deae Cellulose ◽  
Exchange Chromatography ◽  
Galactose Oxidase ◽  
Sedimentation Equilibrium ◽  
Molar Ratio ◽  
Side Chains ◽  
Total Carbohydrate ◽  
Intact Molecule

The articular lubricating fraction from bovine synovial fluid was prepared by repeated fractionation in three consecutive CsCl density gradients to remove completely traces of hyaluronic acid. The major glycoprotein consituent (LGP-I) was then isolated by repeated gel-permeation chromatography. The yield of the LGP-I component was about 20 mg/litre of synovial fluid. Sedimentation-equilibrium measurements showed that this glycoprotein was homogeneous and the mol.wt. was calculated to be 227500. Amino acids represented 43% (w/w) and carbohydrate constituents 44% (w/w) of the molecule. Threonine, glutamic acid, proline and lysine (224, 127, 242 and 128 residues/1000 residues respectively) were the major amino acids. Galactosamine, galactose and N-acetylneuraminic acid (202, 162 and 114 residues/molecule of LGP-I component respectively) accounted for 98% of the total carbohydrate residues present. Small amounts of mannose and glucosamine (1 and 9mol respectively/mol of LGP-I component) were also present. After treatment of LGP-I component with alkali and NaB3H4 radioactivity was incorporated into alpha-aminobutyric acid and alanine in a molar ratio of 4:1, and radioactive galactosaminitol was isolated by ion-exchange chromatography from a cleaved oligosaccharide fraction. These data demonstrate the presence of threonine and serine -O-GalNAc linkages, but only 25% of the theoretical likages involving threonine were cleaved by a beta-elimination reaction. Digestion of LGP-I component with Pronase followed by chromatography on DEAE-cellulose yielded glycopeptide fractions with a similar amino acid and carbohydrate composition to the intact molecule. Treatment of desialylated and intact LGP-I component with galactose oxidase followed by reduction with NaB3H4 revealed the presence of 52mol of terminal galactose in the intact molecule and 153mol of galactose/mol of LGP-I component after treatment with neuraminidase. The data indicate the LGP-I component is composed of a single polypeptide chain containg more than 150 oligaosaccharide side chains composed of O-GaINAc-Gal distributed over the length of the peptide chain and that terminal sialic acid residues are linked to galactose in two-thirds of these side chains.

scholarly journals Protein Associated with Hyaluronic Acid in Ox Synovial Fluid

1969 ◽  
Vol 22 (4) ◽  
pp. 1031 ◽  
Author(s):  
Panee Silpananta ◽  
JR Dunstone ◽  
AG Ogston
Keyword(s):  
Hyaluronic Acid ◽  
Synovial Fluid ◽  
Density Gradient ◽  
Caesium Chloride ◽  
Equilibrium Sedimentation ◽  
Molecular Sizes

Protein which is associated with hyaluronic acid, prepared in a physico-chemically unchanged state from ox synovial fluid by ultrafiltration, has been separated by preparative equilibrium sedimentation in a caesium chloride density gradient and by chromatography on DEAE-Sephadex. Earlier work has been confirmed by showing that the protein consists of at least two chemically distinct lipoprotein, components. It has also been confirmed that its removal from the hyaluronic acid causes marked changes of viscosity, without the occurrence of degradation of the hyaluronic acid. The separated proteins appeared in a number of differently aggregated forms, and this fact has prevented our drawing conclusions about their molecular sizes in synovial fluid.

scholarly journals Fractionation of a hyaluronic acid preparation in a density gradient. Some properties of the hyaluronic acid

1968 ◽  
Vol 109 (1) ◽  
pp. 43-50 ◽  
Author(s):  
Panee Silpananta ◽  
J. R. Dunstone ◽  
A. G. Ogston
Keyword(s):  
Hyaluronic Acid ◽  
Density Gradient ◽  
Chondroitin Sulphate ◽  
Sedimentation Equilibrium ◽  
Partial Specific Volume ◽  
Low Velocity ◽  
Molecular Configuration ◽  
Caesium Chloride ◽  
A Value ◽  
Couette Viscometer

1. Hyaluronic acid was isolated from ox synovial fluid by sedimentation equilibrium in a caesium chloride density gradient (Silpananta, Dunstone & Ogston, 1967). The product was almost free from chondroitin sulphate and from protein. 2. Its composition did not differ significantly from that of the carbohydrate part of the protein-containing material isolated by filtration. Its physicochemical properties and molecular configuration were similar, except for its viscosity, which showed markedly reduced concentration-dependence and shear-dependence. This suggests that the associated protein tends to form links between molecules of hyaluronic acid. 3. The accurate measurement of viscosity at very low velocity gradient, by use of the damping of oscillations in a Couette viscometer, is described. 4. A method is described for measuring, approximately, the thermodynamic non-ideality of a solute from the shape of its schlieren curve at sedimentation equilibrium in a density gradient. 5. A value for the partial specific volume of hyaluronic acid in dilute salt solution was calculated from its isopycnic density in a caesium chloride gradient.

scholarly journals Hyaluronic Acid in Synovial Fluid

1970 ◽  
Vol 11 (2) ◽  
pp. 139-155 ◽  
Author(s):  
Nils W. Rydell ◽  
Judson Butler ◽  
Endre A. Balazs
Keyword(s):  
Hyaluronic Acid ◽  
Synovial Fluid

scholarly journals Advantages of Hyaluronic Acid and Its Combination with Other Bioactive Ingredients in Cosmeceuticals

Molecules ◽  
2021 ◽  
Vol 26 (15) ◽  
pp. 4429
Author(s):  
Anca Maria Juncan ◽  
Dana Georgiana Moisă ◽  
Antonello Santini ◽  
Claudiu Morgovan ◽  
Luca-Liviu Rus ◽  
...  
Keyword(s):  
Hyaluronic Acid ◽  
Glucuronic Acid ◽  
Biological Effects ◽  
Biological Processes ◽  
Cosmetic Products ◽  
Aesthetic Medicine ◽  
Cosmetic Formulations ◽  
Other Substances ◽  
Bioactive Ingredients ◽  
Brand Portfolio

This study proposes a review on hyaluronic acid (HA) known as hyaluronan or hyaluronate and its derivates and their application in cosmetic formulations. HA is a glycosaminoglycan constituted from two disaccharides (N-acetylglucosamine and D-glucuronic acid), isolated initially from the vitreous humour of the eye, and subsequently discovered in different tissues or fluids (especially in the articular cartilage and the synovial fluid). It is ubiquitous in vertebrates, including humans, and it is involved in diverse biological processes, such as cell differentiation, embryological development, inflammation, wound healing, etc. HA has many qualities that recommend it over other substances used in skin regeneration, with moisturizing and anti-ageing effects. HA molecular weight influences its penetration into the skin and its biological activity. Considering that, nowadays, hyaluronic acid has a wide use and a multitude of applications (in ophthalmology, arthrology, pneumology, rhinology, aesthetic medicine, oncology, nutrition, and cosmetics), the present study describes the main aspects related to its use in cosmetology. The biological effect of HA on the skin level and its potential adverse effects are discussed. Some available cosmetic products containing HA have been identified from the brand portfolio of most known manufacturers and their composition was evaluated. Further, additional biological effects due to the other active ingredients (plant extracts, vitamins, amino acids, peptides, proteins, saccharides, probiotics, etc.) are presented, as well as a description of their possible toxic effects.

scholarly journals The Role of Hyaluronic Acid in Cartilage Boundary Lubrication

Cells ◽  
2020 ◽  
Vol 9 (7) ◽  
pp. 1606 ◽  
Author(s):  
Weifeng Lin ◽  
Zhang Liu ◽  
Nir Kampf ◽  
Jacob Klein
Keyword(s):  
Hyaluronic Acid ◽  
Synovial Fluid ◽  
Surface Force ◽  
Force Balance ◽  
New Paradigm ◽  
Low Friction ◽  
Cartilage Surface ◽  
Boundary Lubricant ◽  
Lipid Layers

Hydration lubrication has emerged as a new paradigm for lubrication in aqueous and biological media, accounting especially for the extremely low friction (friction coefficients down to 0.001) of articular cartilage lubrication in joints. Among the ensemble of molecules acting in the joint, phosphatidylcholine (PC) lipids have been proposed as the key molecules forming, in a complex with other molecules including hyaluronic acid (HA), a robust layer on the outer surface of the cartilage. HA, ubiquitous in synovial joints, is not in itself a good boundary lubricant, but binds the PC lipids at the cartilage surface; these, in turn, massively reduce the friction via hydration lubrication at their exposed, highly hydrated phosphocholine headgroups. An important unresolved issue in this scenario is why the free HA molecules in the synovial fluid do not suppress the lubricity by adsorbing simultaneously to the opposing lipid layers, i.e., forming an adhesive, dissipative bridge between them, as they slide past each other during joint articulation. To address this question, we directly examined the friction between two hydrogenated soy PC (HSPC) lipid layers (in the form of liposomes) immersed in HA solution or two palmitoyl–oleoyl PC (POPC) lipid layers across HA–POPC solution using a surface force balance (SFB). The results show, clearly and surprisingly, that HA addition does not affect the outstanding lubrication provided by the PC lipid layers. A possible mechanism indicated by our data that may account for this is that multiple lipid layers form on each cartilage surface, so that the slip plane may move from the midplane between the opposing surfaces, which is bridged by the HA, to an HA-free interface within a multilayer, where hydration lubrication is freely active. Another possibility suggested by our model experiments is that lipids in synovial fluid may complex with HA, thereby inhibiting the HA molecules from adhering to the lipids on the cartilage surfaces.

Glycosaminoglycans from growing antlers of wapiti (Cervus elaphus)

1997 ◽  
Vol 77 (4) ◽  
pp. 715-721 ◽  
Author(s):  
H. H. Sunwoo ◽  
L. Y. M. Sim ◽  
T. Nakano ◽  
R. J. Hudson ◽  
J. S. Sim
Keyword(s):  
Hyaluronic Acid ◽  
Chondroitin Sulfate ◽  
Cervus Elaphus ◽  
Molecular Size ◽  
Enzymatic Digestion ◽  
Gel Chromatography ◽  
Cellulose Acetate Electrophoresis ◽  
Cartilaginous Tissues ◽  
Chondroitin Sulfates ◽  
Velvet Antler

The emerging wapiti industry in North America is based largely on markets for velvet antlers which are used in oriental medicine. Despite the economic opportunity, enthusiasm has been dampened by incomplete understanding of the chemical and pharmacological properties of velvet antler. This study characterizes polysaccharide constituents of glycosaminoglycans in growing antler of wapiti (Cervus elaphus). Glycosaminoglycans were isolated from four sections (tip, upper, middle and base) of growing antlers, and were studied using cellulose acetate electrophoresis, gel electrophoresis, enzymatic digestion and gel chromatography. The tip and upper sections of the antler which are rich in cartilaginous tissues contained chondroitin sulfate as a major glycosaminoglycan with small amounts of hyaluronic acid. In the middle and base sections containing bone and bone marrow, chondroitin sulfate was also a major glycosaminoglycan with small amounts of hyaluronic acid and chondroitinase-ACI resistant materials. More than half of chondroitin sulfate from the middle and base sections had larger molecular size than did the chondroitin sulfates from the tip and upper sections. Key words: Glycosaminoglycans, chondroitin sulfate, antler, wapiti

scholarly journals Isolation of human synovial-fluid hyaluronate by density-gradient ultracentrifugation and evaluation of its protein content

1972 ◽  
Vol 126 (5) ◽  
pp. 1073-1080 ◽  
Author(s):  
Irwin Scher ◽  
David Hamerman
Keyword(s):  
Synovial Fluid ◽  
Density Gradient ◽  
Density Gradient Ultracentrifugation ◽  
Proteolytic Digestion ◽  
Peptide Fragments ◽  
Guanidinium Chloride ◽  
Caesium Chloride ◽  
Normal Human ◽  
Protein Moiety ◽  
Human Synovial Fluid

1. A compound of hyaluronate and protein, called hyaluronate–protein was isolated from pooled human synovial fluids by caesium chloride density-gradient ultracentrifugation. 2. The isolated hyaluronate–protein was labelled with [125I]iodide and the following studies were done. (a) Ultracentrifugation in caesium chloride showed that the protein moiety (125I counts) and hyaluronate (hexuronate) sedimented together in the middle of the gradient. (b) The labelled hyaluronate–protein was treated with trypsin, and ultracentrifugation showed that peptide fragments (125I counts) were dispersed throughout the gradient, indicating proteolytic digestion. Hyaluronate sedimented in the middle of the gradient. (c) The labelled hyaluronate–protein was digested with streptococcal hyaluronidase, and ultracentrifugation showed that hyaluronate fragments were dispersed throughout the gradient, indicating digestion of the polysaccharide. The protein moiety, without attached hyaluronate, now sedimented at the top of the gradient. (d) Ultracentrifugation of labelled hyaluronate–protein in 4m-guanidinium chloride showed that protein and hyaluronate sedimented together. 3. These studies confirm that hyaluronate is combined with a small quantity of protein in normal human synovial fluid. A mild method for the rapid isolation of hyaluronate–protein in good yield is described.

Sign in / Sign up

Export Citation Format

Share Document