Hb VILA REAL [β36(C2)Pro → His] IN ITALY: CHARACTERIZATION OF THE AMINO ACID SUBSTITUTION AND THE DNA MUTATION

Hemoglobin ◽  
2002 ◽  
Vol 26 (1) ◽  
pp. 21-31 ◽  
Author(s):  
Anna Maria Salzano ◽  
Virginia Carbone ◽  
Leonilde Pagano ◽  
Salvatore Buffardi ◽  
Carlo De Rosa ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Substitution ◽  
Dna Mutation

Hb rainier [β145(HC2)Tyr→Cys] in Italy. Characterization of the amino acid substitution and the DNA mutation

Hemoglobin ◽  
1999 ◽  
Vol 23 (2) ◽  
pp. 111-124 ◽  
Author(s):  
V. Carbone ◽  
A. M. Salzano ◽  
L. Pagano ◽  
A. Viola ◽  
S. Buffardi ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Substitution ◽  
Dna Mutation

scholarly journals Diversity of TEM Mutants in Proteus mirabilis

1999 ◽  
Vol 43 (11) ◽  
pp. 2671-2677 ◽  
Author(s):  
R. Bonnet ◽  
C. De Champs ◽  
D. Sirot ◽  
C. Chanal ◽  
R. Labia ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Substitution ◽  
Proteus Mirabilis ◽  
Clinical Isolates ◽  
Amino Acid Substitutions ◽  
First Report ◽  
Conjugative Plasmids ◽  
Extended Spectrum ◽  
Nucleotide Mutation

ABSTRACT In a survey of resistance to amoxicillin among clinical isolates ofProteus mirabilis, 10 TEM-type β-lactamases were characterized: (i) the well-known penicillinases TEM-1 and TEM-2, the extended-spectrum β-lactamases (ESBLs) TEM-3 and TEM-24, and the inhibitor-resistant TEM (IRT) TEM-44 and (ii) five novel enzymes, a penicillinase TEM-57 similar to TEM-1, an ESBL TEM-66 similar to TEM-3, and three IRTs, TEM-65, TEM-73, and TEM-74. The penicillinase TEM-57 and the ESBL TEM-66 differed from TEM-1 and TEM-3, respectively, by the amino acid substitution Gly-92→Asp (nucleotide mutation G-477→A). This substitution could have accounted for the decrease in pIs (5.2 for TEM-57 and 6.0 for TEM-66) but did not necessarily affect the intrinsic activities of these enzymes. The IRT TEM-65 was an IRT-1-like IRT (Cys-244) related to TEM-2 (Lys-39). The two other IRTs, TEM-73 and TEM-74, were related to IRT-1 (Cys-244) and IRT-2 (Ser-244), respectively, and harbored the amino acid substitutions Leu-21→Phe and Thr-265→Met. In this study, the ESBLs TEM-66, TEM-24, and TEM-3 were encoded by large (170- to 180-kb) conjugative plasmids that exhibited similar patterns after digestion and hybridization with the TEM and AAC(6′)I probes. The three IRTs TEM-65, TEM-73, and TEM-74 were encoded by plasmids that ranged in size from 42 to 70 kb but for which no transfer was obtained. The characterization of five new plasmid-mediated TEM-type β-lactamases and the first report of TEM-24 in P. mirabilis are evidence of the wide diversity of β-lactamases produced in this species and of its possible role as a β-lactamase-encoding plasmid reservoir.

scholarly journals Characterization of Nocardithiocin Derivatives Produced by Amino Acid Substitution of Precursor Peptide notG

2019 ◽  
Vol 26 (1) ◽  
pp. 281-290 ◽  
Author(s):  
Kanae Sakai ◽  
Yasumasa Hara ◽  
Masami Ishibashi ◽  
Mai Sakai ◽  
Seiya Kawahara ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Substitution ◽  
Precursor Peptide

Characterization of a new HLA-G allele encoding a nonconservative amino acid substitution in the α3 domain (exon 4) and its relevance to certain complications in pregnancy

2001 ◽  
Vol 53 (1) ◽  
pp. 48-53 ◽  
Author(s):  
Thomas Vauvert F. Hviid ◽  
Ole B. Christiansen ◽  
Jørgen Krogh Johansen ◽  
Ulla Römmelmayer Hviid ◽  
Claus Lundegaard ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Substitution ◽  
Exon 4 ◽  
Domain Exon ◽  
In Pregnancy

scholarly journals Molecular Characterization of rpoBMutations Conferring Cross-Resistance to Rifamycins on Methicillin-Resistant Staphylococcus aureus

1999 ◽  
Vol 43 (11) ◽  
pp. 2813-2816 ◽  
Author(s):  
Thomas A. Wichelhaus ◽  
Volker Schäfer ◽  
Volker Brade ◽  
Boris Böddinghaus
Keyword(s):  
Staphylococcus Aureus ◽  
Amino Acid ◽  
Molecular Characterization ◽  
Amino Acid Substitution ◽  
Methicillin Resistant Staphylococcus Aureus ◽  
Cross Resistance ◽  
Methicillin Resistant ◽  
Low Level ◽  
Level Resistance

ABSTRACT Mutations of the rpoB gene conferring resistance to rifampin were analyzed in 40 methicillin-resistant Staphylococcus aureus isolates obtained from six countries. Interestingly, the majority of clinical isolates showed multiple mutations withinrpoB. The amino acid substitution 481His→Asn was the most prevalent one, capable of conferring low-level resistance on its own. Cross-resistance to rifampin, rifabutin, and rifapentine was demonstrated for all mutants identified. The level of resistance to rifamycins correlated with both the mutation position and type of amino acid substitution.

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