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Results for “lubricating gel”

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6 recordsLinked to original sources

PubMed2026

Wickerhamomyces anomalus Pseudo-Outbreak Associated with Medical Lubricating Gel, South Africa, 2023-2024.

A nationwide investigation identified 426 patients with Wickerhamomyces anomalus fungal cultures in South Africa; most cases clustered during May-November 2023. Case-patients lacked evidence of infection, indicating a pseudo-outbreak. Genomic and laboratory analyses implicated contaminated sterile lubricating gel. A nationwide product recall resulted in a decline in reported cases.

South Africa↗

PubMed1977

[The significance of the characteristics of lubricating jellies in use during transurethral prostate resections with metallic sheaths (author's transl)].

If a metallic sheath is used during a transurethral resection of the prostate with high-frequency currents, the lubricating jelly has to exceed a prescribed conductivity, in order to prevent dangerous current-density spots within the urethra. Furthermore, the mechanical behaviour of the lubricating jelly and the mode of its application have to be considered carefully.

Burns, Electric↗

PubMed1978

Intestinal mucins in health and disease.

Intestinal mucins are complex glycoproteins which are secreted from goblet cells, and form a gel-like covering over the mucosal surface. They are assumed to provide lubrication and protection of the underlying epithelium against potentially injurious chemicals, enzymes, bacteria and dietary constituents. Recent advances in our understanding of mucin structure, secretion and functional properties are reviewed in this paper. Implications for diseases such as cystic fibrosis, peptic ulcer, malignancy and inflammatory bowel disease are briefly discussed.

Carcinoma↗

PubMed1977

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

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.

Amino Acids↗

PubMed1979

Characterization of homogeneous and pseudocomposite homopolymers and copolymers for articular cartilage replacement.

Semicrystalline swollen polymeric networks are prime candidates for biomedical applications. Purity, controlled structure, easy preparation, non-biodegradability and improved mechanical properties are some of their most important characteristics. New articular cartilage simulants in the form of hydrogels with surface hydroxyl groups have been developed and characterized. The mechanical properties and physical behavior of these materials are described by high elastic moduli, ultimate tensile strength and elongation at break, low tear propagation resistance and excellent friction properties. Crystallinities vary between 15% and 35% and the crystallites are stable within the range of practical applications. The hydrogels show no permeability to hyaluronic acid and can be grafted with cationic monomers or polymers to form boundary lubricant layers. Techniques have also been developed for the preparation of deformable pseudocomposites consisting of layers of swollen semicrystalline and amorphous polymer.

Biocompatible Materials↗

PubMed1979

The isolation and properties of a second glycoprotein (LGP-II) from the articular lubricating fraction from bovine synovial fluid.

A high-molecular-weight glycoprotein (LGP-I) was shown [Swann, Sotman, Dixon & Brooks (1977) Biochem. J. 161, 473--485] to be the major constituent in the articular lubricating fraction from bovine synovial fluid. In addition to the LGP-I component, a second glycoprotein (LGP-II) was also present. After fractionation of bovine synovial fluid by sequential sedimentation in CsCl density gradients, the LGP-I and LGP-II components were separated by gel-permeation chromatography. The LGP-II component was then purified by chromatography on DEAE Bio-Gel A and Bio-Gel P-150. The molecular weight of the LGP-II component was 48,800 calculated from sedimentation-equilibrium measurements. Amino acids represented 53% (w/w) and carbohydrate constituents 36% (w/w) of the molecule. Glutamic acid and lysine (144 and 100 residues/1000 residues) were the major amino acids. Glucosamine, mannose, galactose and N-acetylneuraminic acid [representing 8.0, 6.6, 9.5 and 11.9% (w/w) respectively] were the only carbohydrate constituents detected. Immunodiffusion analysis showed that LGP-II component did not form a detectable precipitin line with antiserum to bovine serum. It appears likely, therefore, that this glycoprotein is synthesized by the joint tissues and is not derived from serum.

Amino Acids↗