Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.2.1.36 (hyaluronidase)
 4,606 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Hyaluronan was substituted with tyramine-cellobiose on amino residues exposed after hydrazinolytic N-deacetylation of the polysaccharide. Nonsubstituted amino groups were reacetylated, and the carboxylic hydrazides were removed by treatment with HIO3. The adduct was labeled with 125I before or after coupling to hyaluronan. N-deacetylation increased with prolonged pretreatment with hydrazine, which also reduced the chain length of hyaluronan. Hydrazinolysis for 30 min produced hyaluronan with Mr 2.2-2.9 x 10(5). This material was substituted with varying amounts of tyramine-cellobiose (from 1 per 20 to 1 per 130 disaccharides). Hyaluronan labeled in this way was recognized by Streptomyces hyaluronidase, hyaluronan affinity protein of cartilage proteoglycan, and receptors for specific endocytosis of hyaluronan in liver endothelial cells. Since tyramine-cellobiose is nondegradable and therefore is arrested intralysosomally at the site of uptake, turnover studies of hyaluronan can be easily carried out with this ligand.
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PMID:Preparation of biologically intact radioiodinated hyaluronan of high specific radioactivity: coupling of 125I-tyramine-cellobiose to amino groups after partial N-deacetylation. 307 Nov 84

Dermatan sulfate oligosaccharides having reducing end 2,5-anhydro-d-talose were prepared by partial N-deacetylation of dermatan sulfate polysaccharide with hydrazine followed by deamination with nitrous acid, and the effect of these oligosaccharides on the activity of bovine testicular hyaluronidase was investigated. Hydrolysis activity and transglycosylation activity of this enzyme were assessed in an independent reaction system by analyzing the products by HPLC. Dermatan sulfate oligosaccharides inhibited hyaluronan hydrolysis by bovine testicular hyaluronidase. Kinetic analysis of the hydrolysis reaction revealed that the inhibition mode by dermatan sulfate oligosaccharides was as competitive as that previously shown by chondroitin sulfate oligosaccharides. Transglycosylation of hyaluronan by bovine testicular hyaluronidase, as a reverse reaction of hydrolysis of hyaluronan, was also inhibited. These inhibitory effects were dependent on the dose and sulfation degree of dermatan sulfate.
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PMID:Dermatan sulfate oligosaccharides having reducing end 2, 5-anhydro-d-talose inhibit bovine testicular hyaluronidase activity. 3139 13

A two or one pot synthesis has been used for the reaction of hyaluronic acid (HA) with octadecylamine (C18) and hydrazine (Hy). In both cases, the chemical derivatization involved primary hydroxyl groups of hyaluronic acid and not its carboxyl groups, whose presence is important for receptor interaction. In this way, Hy-HA-C18 derivatives have been obtained with appropriate hydrophobic and hydrophilic character. Their ability to form homogeneous physical hydrogels has been evaluated as well as the possibility to obtain porous sponges through salt leaching technology. Sponges showing the highest porosity, potentially compatible with cell entrapment, have been characterized with regard to their physicochemical and biological properties. Swelling ability under simulated physiological conditions and stability in the absence or in the presence of hyaluronidase have been investigated. Bovine chondrocytes were viable in Hy-HA-C18 sponges as determined with MTS assay and were able to produce collagen and glycosaminoglycans, as assessed by using Masson's trichrome and Alcian blue, respectively. Finally, in vivo degradation of Hy-HA-C18 sponges has been confirmed after subcutaneous implantation in mice until 6 weeks.
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PMID:Construction and evaluation of sponge scaffolds from hyaluronic acid derivatives for potential cartilage regeneration. 3226 86