Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0276640 (TEM)
 20,729 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Four Klebsiella pneumoniae isolates (LB1, LB2, LB3, and LB4) with increased antimicrobial resistance were obtained from the same patient. The four isolates were indistinguishable in biotype, plasmid content, lipopolysaccharide, and DNA analysis by pulse-field gel electrophoresis. Isolate LB1 made TEM-1 and SHV-1 beta-lactamases. Isolates LB2, LB3, and LB4 produced SHV-5 in addition to TEM-1 and SHV-1. MICs of cefoxitin, ceftazidime, and cefotaxime against LB1 were 4, 1, and 0.06 micrograms/ml, respectively. MICs of ceftazidime against K. pneumoniae LB2, LB3, and LB4 were > 256 micrograms/ml, and those of cefotaxime were 2, 4, and 64 micrograms/ml, respectively. MICs of cefoxitin against K. pneumoniae LB2 and LB3 were 4 micrograms/ml, but that against K. pneumoniae LB4 was 128 micrgrams/ml. K. pneumoniae LB4 could transfer resistance to ceftazidime and cefotaxime, but not that to cefoxitin, to Escherichia coli. Isolate LB4 and cefoxitin-resistant laboratory mutants lacked an outer membrane protein of about 35 kDa whose molecular mass, mode of isolation, resistance to proteases, and reaction with a porin-specific antiserum suggested that it was a porin. MICs of cefoxitin and cefotaxime reverted to 4 and 2 micrograms/ml, respectively, when isolate LB4 was transformed with a gene coding for the K. pneumoniae porin OmpK36. We conclude that the increased resistance to cefoxitin and expanded-spectrum cephalosporins of isolate LB4 was due to loss of a porin channel for antibiotic uptake.
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PMID:In vivo selection of porin-deficient mutants of Klebsiella pneumoniae with increased resistance to cefoxitin and expanded-spectrum-cephalosporins. 1137 40

While identifying proteins present in the cytoskeleton and protein body fractions from maize (Zea mays L.) endosperm, a 51 kDa protein was discovered in a fraction containing small (approximately 200 nm in diameter) protein bodies. Based on partial amino acid sequences of V8 protease fragments, degenerate primers were made and fragments of cDNA encoding these partial sequences were cloned. Using 3' and 5' PCR, a full-length cDNA encoding this 51 kDa protein was obtained, which was identified as legumin-1. In other plants, this protein is generally cleaved into 20 and 35 kDa subunits after synthesis. However, SDS-PAGE of both the native and denatured protein indicates that cleavage does not occur in corn endosperm, even though the cleavage site (asparagine) is conserved. The lack of cleavage is presumably because the canonical cleavage sequence downstream from the cleavage site is almost totally absent. levels of transcript and encoded protein were compared in all three varieties and it was shown that both are more abundant in wild-type maize than in opaque-2 or sweet corn. Finally, using TEM, it was shown that the protein apparently occurs in morphologically distinct protein bodies, very similar to the protein bodies in legumes.
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PMID:Uncleaved legumin in developing maize endosperm: identification, accumulation and putative subcellular localization. 1259 62