scholarly journals Amino acid substitution and chemical characterization of a Japanese variant of carbonic anhydrase I: CA I Hiroshima-1 (86 Asp ? Gly)

1981 ◽  
Vol 19 (5-6) ◽  
pp. 535-549 ◽  
Author(s):  
Takeshi Kageoka ◽  
David Hewett-Emmett ◽  
Sharon K. Stroup ◽  
Ya-Shiou L. Yu ◽  
Richard E. Tashian
Keyword(s):  
Amino Acid ◽  
Carbonic Anhydrase ◽  
Amino Acid Substitution ◽  
Chemical Characterization ◽  
Carbonic Anhydrase I

scholarly journals Chemical characterization of a new Japanese variant of carbonic anhydrase I, CA INagasaki 1 (76 Arg?Gln)

1979 ◽  
Vol 17 (5-6) ◽  
pp. 449-460 ◽  
Author(s):  
Kazuaki Goriki ◽  
Richard E. Tashian ◽  
Sharon K. Stroup ◽  
Ya-Shiou L. Yu ◽  
Dag M. Henriksson
Keyword(s):  
Carbonic Anhydrase ◽  
Chemical Characterization ◽  
Carbonic Anhydrase I

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.

The mouse carbonic anhydrase I gene contains two tissue-specific promoters

1989 ◽  
Vol 9 (8) ◽  
pp. 3308-3313
Author(s):  
P Fraser ◽  
P Cummings ◽  
P Curtis
Keyword(s):  
Carbonic Anhydrase ◽  
Splice Acceptor Site ◽  
Acceptor Site ◽  
Exon 2 ◽  
Tissue Specific ◽  
Isolation And Characterization ◽  
Carbonic Anhydrase I ◽  
Erythroleukemia Cells ◽  
Exon 1

We report the isolation and characterization of the mouse carbonic anhydrase I (CAI) gene. Direct RNA sequence analysis of the 5' nontranslated regions of CAI mRNA from mouse colon and mouse erythroleukemia cells demonstrated tissue specificity in the lengths and sequences of CAI transcripts. Analysis of several mouse CAI genomic clones showed that the transcripts arose from a single CAI gene with two tissue-specific promoters and eight exons. CAI transcripts in the colon were found to initiate just upstream of the erythroid exon 2 of the CAI gene region sequence. Erythroid transcripts originated from a novel promoter upstream of exon 1, which was located more than 10 but less than 250 kilobases upstream of exon 2. Erythroid exon 1 contained only a nontranslated sequence, which was spliced to exon 2 via a cryptic splice acceptor site located in the region that encoded the colon mRNA 5' nontranslated sequence. The remaining exon-intron junctions were conserved in comparison with those of the CAII and CAIII genes.

scholarly journals Erythrocytosis Secondary to Increased Oxygen Affinity of a Mutant Hemoglobin, Hemoglobin Kempsey

Blood ◽  
1968 ◽  
Vol 31 (5) ◽  
pp. 623-632 ◽  
Author(s):  
CON S. REED ◽  
ROGER HAMPSON ◽  
SUSAN GORDON ◽  
RICHARD T. JONES ◽  
MILES J. NOVY ◽  
...  
Keyword(s):  
Amino Acid ◽  
Structure Function ◽  
Autosomal Dominant ◽  
Oxygen Affinity ◽  
Chemical Characterization ◽  
Single Amino Acid ◽  
Genetic Transmission ◽  
Australian Family ◽  
Abnormal Hemoglobin

Abstract An abnormal hemoglobin, termed hemoglobin Kempsey, was found in association with erythrocytosis in ten members of an Australian family. Genetic transmission fits an autosomal dominant pattern. Chemical characterization of hemoglobin Kempsey identified a single amino acid substitution, β99Asp→Asn. Properties of hemoglobin Kempsey include a marked increase in oxygen affinity, retention of the Bohr effect, and decreased heme-heme interaction. Possible structure-function relations of this and other abnormal hemoglobins associated with erythrocytosis are discussed.

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 Partial Chemical Characterization of S-Carboxymethylated Chains of Rabbit Fibrin(OGEN): Evidence for Separate Chain Biosynthesis

1977 ◽  
Author(s):  
B. Alving ◽  
G. Murano ◽  
D. Walz
Keyword(s):  
Amino Acid ◽  
Specific Activity ◽  
Chemical Characterization ◽  
Molecular Size ◽  
Exchange Chromatography ◽  
12 Steps ◽  
Polypeptide Chains ◽  
Sds Electrophoresis ◽  
Derivatives Of

The purpose of this study was twofold: 1) chemically characterize the isolated polypeptide chains of rabbit fibrin(ogen), and 2) explore their mode of biosynthesis. The three S-carboxy-methyl polypeptide chain derivatives of rabbit fibrin (α, β and γ) were isolated by cation exchange chromatography. Their amino acid composition was similar to the human with a methionine distribution (mole/mole) as follows: γ = 9; β = 14, α = 14. Their molecular size, (SDS electrophoresis) was estimated as follows: γ = 46,000; β = 54,000; α = 63,500. The N-terminal amino acid sequence (12 steps) of the β derivative was:Gly-His-Arg-Pro-Ile-Asp-Arg-Arg-Arg-Glu-Glu-Leu-. To determine whether the three chains are synthesized sequentially (one continuous chain, later split into three) or in parallel, turpentine-stimulated male New Zealand rabbits were given ~40 μCi of [75Se] selenomethionine (SeM) and its incorporation into fibrinogen (F) was followed. F was clotted from plasma samples, washed, reduced, and constituent chains separated by gel electrophoresis in the presence of SDS-urea. The radioactivity of each chain (expressed as percent of total F radioactivity) was determined, and the specific methionine radioactivity calculated for each chain isolated at 20, 25, and 30 min after SeM injection. During this interval the specific activity of the α and the γ chains was essentially the same (within 3%) while that of the β chain was 42 to 97% greater than that of the α chain. The similar activity of the α and γ chains during the early phase of SeM incorporation suggests that these two chains are not synthesized sequentially, rather they are synthesized in parallel.

scholarly journals Synthesis and human carbonic anhydrase I, II, VA, and XII inhibition with novel amino acid–sulphonamide conjugates

2020 ◽  
Vol 35 (1) ◽  
pp. 489-497 ◽  
Author(s):  
Hasan Küçükbay ◽  
Nesrin Buğday ◽  
F. Zehra Küçükbay ◽  
Andrea Ageli ◽  
Gianluca Bartolucci ◽  
...  
Keyword(s):  
Amino Acid ◽  
Carbonic Anhydrase ◽  
Carbonic Anhydrase I ◽  
Human Carbonic Anhydrase
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