Characterization of the amino acid change in a transferrin variant

1988 ◽  
Vol 16 (5) ◽  
pp. 834-835 ◽  
Author(s):  
ROBERT W. EVANS ◽  
ANDREW MEILAK ◽  
ALASTAIR AITKEN ◽  
KOKILA J. PATEL ◽  
COLLIN WONG ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Change

scholarly journals Frataxin-bypassing Isu1: characterization of the bypass activity in cells and mitochondria

2014 ◽  
Vol 459 (1) ◽  
pp. 71-81 ◽  
Author(s):  
Heeyong Yoon ◽  
Simon A. B. Knight ◽  
Alok Pandey ◽  
Jayashree Pain ◽  
Yan Zhang ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Change ◽  
Scaffold Protein ◽  
Cluster Assembly ◽  
Cysteine Desulfurase ◽  
In Cells

The Fe–S cluster assembly scaffold protein Isu1 with the amino acid change M107I is able to bypass lack of the frataxin by stimulating cysteine desulfurase activity in mitochondria, although a kinetic defect in Fe–S cluster assembly persists.

scholarly journals Molecular Characterization of Fluoroquinolone-Resistant Bartonella bacilliformis

Pathogens ◽  
2021 ◽  
Vol 10 (7) ◽  
pp. 876
Author(s):  
Giovanna Mendoza-Mujica ◽  
Diana Flores-León ◽  
Joaquim Ruiz
Keyword(s):  
Amino Acid ◽  
Molecular Characterization ◽  
Amino Acid Change ◽  
23S Rrna ◽  
Amino Acid Substitutions ◽  
Bartonella Bacilliformis ◽  
Chloramphenicol Resistance ◽  
Ciprofloxacin Resistance ◽  
Double Substitution

The presence of amino acid changes in GyrA, GyrB, ParC, ParE, and in a proposed chromosomal chloramphenicol acetyl transferase (CAT), as well as mutations at 23S rRNA, were established by PCR and sequencing in 38 B. bacilliformis clinical isolates from four different areas in Peru. Eighteen out of 24 (75%) isolates showing ciprofloxacin resistance for both disk-diffusion and e-test presented amino acid substitutions in GyrA (G89C, six isolates, A91V, 1 isolate) GyrB (S474F, 10 isolates) or both (GyrA D95N and GyrB S474F, one isolate). Two out of 14 susceptible isolates presented amino acid substitutions at GyrB (S474F) or a double substitution GyrA D95N and GyrB S474F. Of note, ciprofloxacin-resistant isolates were recovered in the four areas studied. No amino acid change was observed at ParC or ParE. Only one isolate showed chloramphenicol resistance, but no alteration was present in either 23S rRNA or CAT. B. bacilliformis resistant to quinolones are extended throughout Peru, with amino acid substitutions at GyrA or GyrB as the main, albeit not exclusive, cause. B. bacilliformis seems to have an apparent facility to develop mutations on GyrB outside the classical positions 91, 95 of GyrA and 85, 88 of ParC.

PURIFICATION AND PARTIAL CHEMICAL CHARACTERIZATION OF SHEEP NEUROPHYSIN

1973 ◽  
Vol 74 (2) ◽  
pp. 226-236 ◽  
Author(s):  
Michel Chrétien ◽  
Claude Gilardeau
Keyword(s):  
Amino Acid ◽  
Polyacrylamide Gel Electrophoresis ◽  
Chemical Characterization ◽  
Terminal Amino Acid ◽  
Amino Acid Determination ◽  
Pituitary Glands ◽  
Terminal Amino ◽  
Partial Chemical ◽  
Acid Determination

ABSTRACT A protein isolated from ovine pituitary glands has been purified, and its homogeneity assessed by NH2- and COOH-terminal amino acid determination, ultracentrifugation studies, and polyacrylamide gel electrophoresis after carboxymethylation. Its chemical and immunochemical properties are closely similar to those of beef and pork neurophysins, less similar to those of human neurophysins. It contains no tryptophan (like other neurophysins) or histidine (like all except bovine neurophysin-I and human neurophysins). It has alanine at the NH2-terminus and valine at the COOH-terminus. Its amino acid composition is similar to, but not identical with those of porcine and bovine neurophysins.

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