Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0348321 (Haemophilus)
 15,372 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

We have defined the nature of the covalent linkages in a Haemophilus influenzae type b oligosaccharide-CRM197 conjugate vaccine, designated HbOC. The conjugate was acid hydrolyzed to release a novel amino-acid derivative, N epsilon-(2-hydroxyethyl)lysine (OHEt-Lys), identifiable with an amino-acid analyzer. This amino-acid derivative was formed by reduction of Schiff bases formed between H. influenzae type b oligosaccharides (HbO) and the lysyl epsilon-amino groups of CRM197 (a non-toxic, cross-reactive variant of diphtheria toxin), followed by acid hydrolysis of HbOC. Quantification of OHEt-Lys per CRM197 molecule allowed the determination of a covalency ratio, a useful parameter for evaluating the stoichiometry and consistency of HbOC preparations. Covalent association between HbO and CRM197 was also demonstrated by the coincidence of immunoreactivity of gel-electrophoresed HbOC on a Western blot probed with anti-CRM197 and anti-saccharide antisera.
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PMID:Chemical evidence for covalent linkages of a semi-synthetic glycoconjugate vaccine for Haemophilus influenzae type B disease. 253 95

The susceptibilities of strains of Gardnerella vaginalis (Haemophilus vaginalis), Neisseria gonorrhoeae, and Bacteroides fragilis to metronidazole and its principal oxidative metabolites (1-[2-hydroxyethyl]-2-hydroxymethyl-5-nitroimidazole) ("hydroxy" metabolite) and 1-acetic acid-2-methyl-5-nitroimidazole ("acid" metabolite), were compared by determinations of the minimal inhibitory concentrations (MICs) of these compounds. Against ten strains of G. vaginalis, the hydroxy metabolite was the most active (median MIC, 2 microgram/ml); the median MICs of metronidazole and of the acid metabolite were 8 and 64 microgram/ml, respectively. The hydroxy metabolite was also the most active against 15 strains of N. gonorrhoeae (median MIC, 32 microgram/ml). In contrast, metronidazole was the most active against ten strains of B. fragilis (median MIC, 1 microgram/ml); the hydroxy and acid metabolites had median MICs of 2 and 64 micrograms/ml, respectively. These results indicate that in the treatment of G. vaginalis-associated vaginitis with metronidazole, the hydroxy metabolite may contribute a significant antimicrobial effect, in view of its excellent activity in vitro.
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PMID:Relative susceptibilities of Gardnerella vaginalis (Haemophilus vaginalis), Neisseria gonorrhoeae, and Bacteroides fragilis to Metronidazole and its two major metabolites. 677 87

The cDNA for the rat cytosolic branched chain aminotransferase (BCATc) has been cloned. The BCATc cDNA encodes a polypeptide of 410 amino acids with a calculated molecular mass of 46.0 kDa. By Northern blot analysis, BCATc message of approximately 2.7 kilobases was readily detected in rat brain, but was absent from liver, a rat hepatoma cell line, kidney, and skeletal muscle. When expressed in COS-1 cells, the enzyme is immunologically indistinguishable from the native enzyme found in rat brain cytosol. Comparison of the rat BCATc sequence with available data bases identified the Escherichia coli (and Salmonella typhimurium) branched chain aminotransferase (BCAT) and revealed a Haemophilus influenzae BCAT, a yeast BCAT, which is hypothesized to be a mitochondrial form of the enzyme, and the murine BCATc (protein ECA39). Calculated molecular masses for the complete proteins are 33.9 kDa, 37.9 kDa, 42.9 kDa, and 43.6 kDa, respectively. The rat BCATc sequence was 84% identical with murine BCATc, 45% identical with yeast, 33% identical with H. influenzae, 27% identical with the E. coli and S. typhimurium BCAT, and 22% identical with the evolutionary related D-amino acid aminotransferase (D-AAT) (Tanizawa, K., Asano, S., Masu, Y., Kuramitsu, S., Kagamiyama, H., Tanaka, H., and Soda, K. (1989) J. Biol. Chem. 264, 2450-2454). Amino acid sequence alignment of BCATc with D-AAT suggests that the folding pattern of the overlapping mammalian BCATc sequence is similar to that of D-AAT and indicates that orientation of the pyridoxal phosphate cofactor in the active site of the eukaryotic BCAT is the same as in D-AAT. Thus, BCAT are the only eukaryotic aminotransferases to abstract and replace the proton on the re face of the pyridoxal phosphate cofactor. Finally, requirements for recognition of substrate L-amino acid and alpha-carboxylate binding are discussed.
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PMID:Cloning and expression of the mammalian cytosolic branched chain aminotransferase isoenzyme. 853 Apr 59