scholarly journals Enolase isoenzymes in adult and developing Xenopus laevis and characterization of a cloned enolase sequence

1988 ◽  
Vol 251 (1) ◽  
pp. 31-39 ◽  
Author(s):  
N Segil ◽  
A Shrutkowski ◽  
M B Dworkin ◽  
E Dworkin-Rastl
Keyword(s):  
Amino Acid ◽  
Nucleotide Sequence ◽  
Xenopus Laevis ◽  
Adult Brain ◽  
Gene Products ◽  
Adult Liver ◽  
Acidic Form ◽  
High Concentrations ◽  
Enolase Gene Eno1

As part of a study of glycolysis during early development we have examined the pattern of expression of enolase isoenzymes in Xenopus laevis. In addition, the nucleotide sequence of a cDNA clone coding for the complete amino acid sequence of one enolase gene (ENO1) in X. laevis was determined. X. laevis ENO1 shows highest homology to mammalian non-neuronal enolase. Analysis of enolase isoenzymes in X. laevis by non-denaturing electrophoresis on cellulose acetate strips revealed five isoenzymes. One form was present in all tissues tested, two additional forms were expressed in oocytes, embryos, adult liver and adult brain, and two further forms were restricted to larval and adult muscle. Since enolase is a dimer, three different monomers (gene products) could account for the observed number of isoenzymes. This pattern of enolase isoenzyme expression in X. laevis differs from that of birds and mammals. In birds and mammals the most acidic form is neuron-specific and there is only one major isoenzyme expressed in the liver. RNAase protection experiments showed the presence of ENO1 mRNA in oocytes, liver and muscle, suggesting that it codes for a non-tissue-restricted isoenzyme. ENO1 mRNA concentrations are high in early oocytes, decrease during oogenesis and decrease further after fertilization. Enolase protein, however, is maintained at high concentrations throughout this period.

scholarly journals Nucleotide Sequence and Characterization of a Novel Cefotaxime-Hydrolyzing β-Lactamase (CTX-M-10) Isolated in Spain

2001 ◽  
Vol 45 (2) ◽  
pp. 616-620 ◽  
Author(s):  
Antonio Oliver ◽  
José Claudio Pérez-Dı́az ◽  
Teresa M. Coque ◽  
Fernando Baquero ◽  
Rafael Cantón
Keyword(s):  
Amino Acid ◽  
Nucleotide Sequence ◽  
Amino Acid Sequence Identity ◽  
Penicillin G ◽  
Nucleotide Substitutions ◽  
Sequence Identity ◽  
M 10 ◽  
Hydrolysis Rates ◽  
Kluyvera Ascorbata

ABSTRACT A cefotaxime-resistant, ceftazidime-susceptible Escherichia coli isolate was obtained from a patient with sepsis in 1997, from which a β-lactamase with a pI of 8.1 was cloned. Cephaloridine and cefotaxime relative hydrolysis rates were 167 and 81, respectively (penicillin G rate = 100), whereas ceftazidime hydrolysis was not detected. The nucleotide sequence revealed a bla gene related to that coding for CTX-M-3. Despite 21 nucleotide substitutions, only 2 determined amino acid changes (Ala27Val and Arg38Gln). The amino acid sequence identity between this enzyme, designated CTX-M-10, and the chromosomal β-lactamase ofKluyvera ascorbata was 81%.

scholarly journals Molecular Characterization of an Avian Astrovirus

2000 ◽  
Vol 74 (13) ◽  
pp. 6173-6177 ◽  
Author(s):  
Matthew D. Koci ◽  
Bruce S. Seal ◽  
Stacey Schultz-Cherry
Keyword(s):  
Amino Acid ◽  
Nucleotide Sequence ◽  
Amino Acid Sequence ◽  
Animal Species ◽  
Genomic Organization ◽  
Predicted Amino Acid Sequence ◽  
Enteric Disease ◽  
Nucleotide Level ◽  
Human Astroviruses

ABSTRACT Astroviruses are known to cause enteric disease in several animal species, including turkeys. However, only human astroviruses have been well characterized at the nucleotide level. Herein we report the nucleotide sequence, genomic organization, and predicted amino acid sequence of a turkey astrovirus isolated from poults with an emerging enteric disease.

scholarly journals Identification of Residues of the Kid Toxin Involved in Autoregulation of the parD System

2004 ◽  
Vol 186 (1) ◽  
pp. 240-243 ◽  
Author(s):  
Marc Lemonnier ◽  
Sandra Santos-Sierra ◽  
Consolación Pardo-Abarrio ◽  
Ramón Díaz-Orejas
Keyword(s):  
Amino Acid ◽  
Single Amino Acid ◽  
Gene Products ◽  
Coordinated Action ◽  
Plasmid R1 ◽  
In Vivo Characterization

ABSTRACT The toxin-antitoxin system parD (kis kid) of plasmid R1 is coregulated by the coordinated action of its two gene products. Here we describe the isolation and the in vivo characterization of three single-amino-acid changes in the Kid toxin, G4E, C74Y, and E91K, that affect the coregulatory activity but preserve the toxicity of the protein.

scholarly journals Molecular characterization of three newly recognized rat parvoviruses

2002 ◽  
Vol 83 (8) ◽  
pp. 2075-2083 ◽  
Author(s):  
Cho-Hua Wan ◽  
Maria Söderlund-Venermo ◽  
David J. Pintel ◽  
Lela K. Riley
Keyword(s):  
Amino Acid ◽  
Nucleotide Sequence ◽  
Molecular Characterization ◽  
Amino Acid Sequences ◽  
Minute Virus ◽  
Genomic Nucleotide Sequence ◽  
Kilham Rat Virus

Rodent parvoviruses have been documented to interfere with both in vivo and in vitro research. In this study, three rat parvoviruses distinct from previously characterized rodent parvoviruses were identified from naturally infected rats obtained from four discrete sources. These three newly recognized parvoviruses were designated rat minute virus (RMV)-1a, -1b and -1c. In this study, the genomic nucleotide sequence and the predicted amino acid sequences of proteins for each of the three RMV-1 variants and Kilham rat virus (KRV) were determined and compared with previously characterized rodent parvoviruses. The three RMV-1 variants were shown to be closely related to each other, to be distinct from but closely related to KRV and H-1 virus, and to be significantly different from the previously identified rat parvovirus isolate, RPV-1a.

Porcine d-amino acid Oxidase: Determination of the mRNA nucleotide sequence by the characterization of genomic and cDNA clones

Gene ◽  
1987 ◽  
Vol 59 (1) ◽  
pp. 55-61 ◽  
Author(s):  
P. Jacobs ◽  
F. Brockly ◽  
M. Massaer ◽  
R. Loriau ◽  
J.P. Guillaume ◽  
...  
Keyword(s):  
Amino Acid ◽  
Nucleotide Sequence ◽  
Cdna Clones ◽  
Acid Oxidase ◽  
Amino Acid Oxidase

scholarly journals Cloning of the gene coding for human class 1 heparin-binding growth factor and its expression in fetal tissues.

1989 ◽  
Vol 9 (6) ◽  
pp. 2387-2395 ◽  
Author(s):  
W P Wang ◽  
K Lehtoma ◽  
M L Varban ◽  
I Krishnan ◽  
I M Chiu
Keyword(s):  
Amino Acid ◽  
Growth Factor ◽  
Nucleotide Sequence ◽  
Amino Acid Sequence ◽  
Genomic Dna ◽  
Adult Brain ◽  
Heparin Binding ◽  
Human Class ◽  
Gene Coding ◽  
Class 1

We have identified four overlapping genomic DNA clones coding for human class 1 heparin-binding growth factor (HBGF-1), also known as acidic fibroblast growth factor, by screening genomic DNA libraries with an HBGF-1 cDNA probe. The exon-intron structure of the HBGF-1 gene was determined by Southern hybridization and nucleotide sequence analysis. The complete amino acid sequence of human HBGF-1 was deduced from the nucleotide sequence of these genomic DNA clones. The predicted amino acid sequence is identical to the published amino acid sequence determined by protein sequencing. Southern blot analysis of human DNA suggested that there is a single-copy gene coding for HBGF-1. A 4.5-kilobase mRNA and two minor species (3.4 and 2.0 kilobases) homologous to the HBGF-1 gene were detected in cellular RNA isolated from human adult brain and kidney. The HBGF-1 mRNAs from brain and kidney had slightly different sizes. The mechanism for the synthesis of different sizes of mRNA was not determined. We also detected HBGF-1 transcript from glioblastoma cells, fetal brain, and kidney but not from placenta or fetal liver. Since HBGF-1 is an angiogenic factor, these data suggest that it may play a role in embryonic angiogenesis during fetal development.

Nucleotide sequence of the nifLA operon of Klebsiella oxytoca NG13 and characterization of the gene products

1986 ◽  
Vol 205 (2) ◽  
pp. 253-259 ◽  
Author(s):  
Young-Mi Kim ◽  
Kyung-Joon Ahn ◽  
Teruhiko Beppu ◽  
Takeshi Uozumi
Keyword(s):  
Nucleotide Sequence ◽  
Klebsiella Oxytoca ◽  
Gene Products

scholarly journals Functional characterization of alternatively spliced human SERCA3 transcripts

1998 ◽  
Vol 275 (6) ◽  
pp. C1449-C1458 ◽  
Author(s):  
Esteban Poch ◽  
Stephen Leach ◽  
Susan Snape ◽  
Tasha Cacic ◽  
David H. MacLennan ◽  
...  
Keyword(s):  
Amino Acids ◽  
Monoclonal Antibody ◽  
Endoplasmic Reticulum ◽  
Amino Acid ◽  
Functional Characterization ◽  
Lymphoid Tissues ◽  
Gene Products ◽  
Alternatively Spliced ◽  
Lower Capacity

The sarcoplasmic (or endoplasmic) reticulum Ca2+-ATPase (SERCA)-3 has been implicated in the possible dysregulation of Ca2+ homeostasis that accompanies the pathology of hypertension and diabetes. We report the molecular cloning of two alternatively spliced transcripts from the human SERCA3 gene, ATP2A3, that encode proteins that differ at their carboxy termini by 36 amino acids. SERCA3 transcripts were most abundantly expressed in lymphoid tissues, intestine, pancreas, and prostate. The two human SERCA3 proteins encoded by alternatively spliced transcripts were recognized by the monoclonal antibody PL/IM430 and demonstrated Ca2+ uptake and ATPase activity with an apparent Ca2+ affinity 0.5 pCa unit lower than that of other SERCA gene products. The subcellular distribution of SERCA3 protein was indistinguishable from that of SERCA2b, with expression in the nuclear envelope and in the endoplasmic reticulum throughout the cell. Two variant SERCA3 constructs, huS3-I and huS3-II, were isolated that encode proteins with three amino acid differences: Ala-673 (in huS3-I) substituted for Thr (in huS3-II), Ile-817 substituted for Met, and an insertion of Glu-994. huS3-I displayed a 10-fold lower capacity to transport Ca2+ than huS3-II.

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