Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.2.1.17 (lysozyme)
 21,489 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Galactose, lactose, N-acetylgalactosamine, N-acetylglucosamine and fibrinoglycopeptides were bound to lysozyme by different linkages. These glycosylated lysozymes were tested as N-acetylneuraminic acid acceptors using particular sialytransferase preparations from frog and bovine liver and from bovine and porcine submandibular glands. Desialylated fetuin served as reference compound. Galactose residues of desialo-fetuin and lysozyme-lactose are sialylated by all four sialytransferases tested, galactose bound to lysozyme via a phenylazo group is inactive with the enzyme from bovine submandibular gland, and galactose bound directly to lysozyme serves as substrate only for the frog liver sialytransferase. Lysozyme-phenylazo-N-acetylgalactosamine is active only with the sialytransferase from bovine sumbandibular gland. N-Acetylglucosamine derivatives of lysozyme are inactive with all sialytransferases tested. These observations are discussed in the light of the natural substrates for the sialytransferases investigated.
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PMID:The specificity of sialytransferases using glycosylated lysozyme derivatives as substrates. 51 Oct 94

The Streptococcus mutans group b antigen of strain FA1 has been defined as to chemical composition and immunological specificity. The antigen in cold trichloroacetic acid extracts was fractionated on diethylaminoethyl-Sephadex A-25 at pH 8.5. Two forms were isolated: a polysaccharide and a mucoprotein. The two polymers reacted as a single substance in agar gel diffusion against specific adsorbed FA1 rabbit antisera but were separated by gel immunoelectrophoresis. No reaction with any other S. mutans or streptococcal group sera occurred. Galactose composed about one-third and galactosamine about 3% of the total weight of each polymer. Rhamnose was a major component of the polysaccharide (47%) but was present only in traces in the mucoprotein. The protein content of the latter was about 40%. No significant quantities of glycerol, phosphorus, or muramic acid were present in either case. Pepsin and trypsin had no effect on the serological specificity of the mucoprotein. d-Galactose and d-galactosamine were strong inhibitors (70%) of the precipitin reaction, whereas d-glucose, d-glucosamine, and N-acetyl-d-glucosamine inhibited between 25 and 35%. The results indicate that the antigen is a major antigenic component of the cell wall and that the specificity of the antigen resides in binding sites which contain both d-galactose and d-galactosamine. Agglutination of whole cells by specific group b antiserum indicates the antibody receptor sites of the polysaccharide antigen are at the surface of the streptococcal cell. The mucoprotein, but not the polysaccharide, was released from the cell by lysozyme. Lysis did not occur. The immunological specificity and other characteristics of the antigen establishes it as the identifying antigen of S. mutans group b.
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PMID:Structure and immunological specificity of the Streptococcus mutans group b cell wall antigen. 412 3

The capsular polysaccharide (CPS) of Streptococcus (S.) suis type 2 was isolated from a type strain of S. suis NCTC 10234 by three different preparative methods: (A) lysozyme treatment method, (B) autoclave extraction method, and (C) HCl-extraction method. The structural characteristics of the three CPS (CPS-A, B and C) were examined by gel permeation chromatography, reactivity against rabbit antiserum and proton-nuclear magnetic resonance (1H-NMR). N-Acetylneuraminic acid (NeuAc) residues as sialic acid in CPS-C were partially dissociated or degraded during preparation with a remarkable decrease in the molecular mass and the antigen activity. Although both methods A and B produced intact CPS without releasing NeuAc residues, method B was considered to be a more suitable procedure for preparing the CPS antigen because of time-saving and safety factors. Sugar analysis by high performance liquid chromatography and gas liquid chromatography showed that CPS-B consisted of five kinds of sugars: Rhamnose (Rha), Glucose (Glc). Galactose (Gal), N-acetylglucosamine (GlcNAc) and NeuAc, in a molar ratio of 1.00:0.95:3.68:0.80:1.31. After complete removal of NeuAc residues by mild acid hydrolysis of CPS-B, the reactivity with anti-type 2 serum was not detected. The NeuAc residue in CPS of S. suis type 2 strain was thought to be the antigen epitope portion.
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PMID:Comparative preparation methods of sialylated capsule antigen from Streptococcus suis type 2 with type specific antigenicity. 891 93