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)

Recently we purified to homogeneity hyaluronidase from stonefish (Synanceja horrida) venom, for the first time from a marine source [Poh, Yuen, Chung & Khoo (1992) Comp. Biochem. Physiol., in the press]. In the present study the reaction products of the hyaluronidase purified from stonefish venom were analysed. It produced tetra-, hexa-, octa- and deca-saccharides as major end products, but not disaccharides. The structure of the tetrasaccharide product was determined by enzymic analysis, in conjunction with h.p.l.c. and by 1H n.m.r., as GlcA beta 1-3GlcNAc beta 1-4GlcA beta 1-3GlcNAc. Chemical shifts of the structural-reporter-group protons of the constituent monosaccharides for the tetrasaccharide have been assigned. The enzyme did not act on chondroitin sulphate or dermatan sulphate. The results indicate that the stonefish hyaluronidase is an endo-beta-N-acetylglucosaminidase specific for hyaluronate.
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PMID:Identification of the reaction products of the purified hyaluronidase from stonefish (Synanceja horrida) venom. 156 84

The chain length of [3H]hyaluronic acid synthesized by cultivating human skin fibroblasts in the presence of [3H]glucosamine was investigated. [3H]Hyaluronic acid obtained from the matrix fraction was excluded from a Sepharose CL-2B column irrespective of the incubation period, whereas that from the medium was depolymerized into a constant chain length (Mr = 40,000). The reducing and non-reducing terminals of the depolymerized hyaluronic acid were N-acetylglucosamine and glucuronic acid, respectively. Prolonged incubation produced no oligosaccharides as shown by examination of hyaluronidase digests, suggesting the presence of a novel endo-beta-N-acetylglucosaminidase in cultured human skin fibroblasts.
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PMID:Extracellular depolymerization of hyaluronic acid in cultured human skin fibroblasts. 222 83

A recombinant lambda phage was identified in a Clostridium perfringens genomic library by means of its ability to hydrolyse the fluorescent substrate 4-methyl-umbelliferyl-beta-D-glucosaminide, isolated and shown to encode an endo-beta-N-acetylglucosaminidase. This enzyme, NagH, is also known as hyaluronidase, or Mu toxin, a putative virulence factor which is likely to act on connective tissue during gas gangrene. Nucleotide sequence analysis allowed the primary structure to be deduced and showed hyaluronidase to be a large exported protein of 114,392 Daltons and an enzyme of this size, endowed with the corresponding activities, was partially purified from C. perfringens. Hyaluronidase seems to be organised into two domains, an N-terminal region comprising 700 amino acids bearing the active site and a 300-residue C-terminal segment, containing three copies of an extended motif. Two other reading frames, linked to nagH, also appear to encode proteins with sugar-binding motifs.
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PMID:Molecular genetic analysis of the nagH gene encoding a hyaluronidase of Clostridium perfringens. 817 18