Human Phenylalanyl-tRNA Synthetase: Cloning, Characterization of the Deduced Amino Acid Sequences in Terms of the Structural Domains and Coordinately Regulated Expression of the α and β Subunits in Chronic Myeloid Leukemia Cells

1999 ◽  
Vol 255 (3) ◽  
pp. 765-773 ◽  
Author(s):  
Marianna Rodova ◽  
Valentina Ankilova ◽  
Mark G. Safro
Keyword(s):  
Amino Acid ◽  
Chronic Myeloid Leukemia ◽  
Myeloid Leukemia ◽  
Trna Synthetase ◽  
Amino Acid Sequences ◽  
Leukemia Cells ◽  
Structural Domains ◽  
Regulated Expression ◽  
Α And Β Subunits

scholarly journals Transcriptomics-Based Characterization of the Toxicity of ZnO Nanoparticles Against Chronic Myeloid Leukemia Cells

2020 ◽  
Vol Volume 15 ◽  
pp. 7901-7921
Author(s):  
Suliman A Alsagaby ◽  
Rajendran Vijayakumar ◽  
Mariappan Premanathan ◽  
Suresh Mickymaray ◽  
Wael Alturaiki ◽  
...  
Keyword(s):  
Chronic Myeloid Leukemia ◽  
Zno Nanoparticles ◽  
Myeloid Leukemia ◽  
Leukemia Cells

scholarly journals Purification and characterization of a ubenimex (Bestatin)-sensitive aminopeptidase B-like enzyme from K562 human chronic myeloid leukemia cells

FEBS Letters ◽  
1994 ◽  
Vol 342 (1) ◽  
pp. 53-56 ◽  
Author(s):  
Masatoshi Yamada ◽  
Yoshikazu Sukenaga ◽  
Hideji Fujii ◽  
Fuminori Abe ◽  
Tomio Takeuchi
Keyword(s):  
Chronic Myeloid Leukemia ◽  
Myeloid Leukemia ◽  
Leukemia Cells ◽  
Purification And Characterization

Characterization of Glycoprotein Fraction from Carp Pituitaries Isolated Using Concanavalin A as the Affinity Ligand

1998 ◽  
Vol 63 (3) ◽  
pp. 434-440 ◽  
Author(s):  
Irena Hulová ◽  
Jana Barthová ◽  
Helena Ryšlavá ◽  
Václav Kašička
Keyword(s):  
Concanavalin A ◽  
Reversed Phase ◽  
Amino Acid Sequences ◽  
Gel Chromatography ◽  
Affinity Ligand ◽  
Sds Page ◽  
Terminal Amino ◽  
Α And Β Subunits

Glycoproteins that have affinity to Concanavalin A were isolated from the acetone-dried pituitaries of common carp (Cyprinus carpio L.). Two fractions of glycoproteins were separated using gel chromatography on Superdex 75HR. The fraction with lower molecular weight (30 000) corresponding to the carp gonadotropin cGtH II was composed of two subunits as determined using SDS-PAGE. This protein fraction was further divided into four components using reversed-phase HPLC. Two fractions were pure α and β subunits of cGtH II as follows from immunodetection and from determination of N-terminal amino acid sequences. The other two were a mixture of α and β subunits as was also revealed by N-terminal analysis. Capillary electrophoresis was also used for characterization of isolated glycoproteins.

scholarly journals ST1926, an orally active synthetic retinoid, induces apoptosis in chronic myeloid leukemia cells and prolongs survival in a murine model

2015 ◽  
Vol 137 (3) ◽  
pp. 698-709 ◽  
Author(s):  
Rihab R. Nasr ◽  
Raed A. Hmadi ◽  
Rabab M. El-Eit ◽  
Ahmad N. Iskandarani ◽  
Mark N. Jabbour ◽  
...  
Keyword(s):  
Chronic Myeloid Leukemia ◽  
Murine Model ◽  
Myeloid Leukemia ◽  
Leukemia Cells ◽  
Synthetic Retinoid ◽  
Orally Active

scholarly journals Characterization of the Gallate Dioxygenase Gene: Three Distinct Ring Cleavage Dioxygenases Are Involved in Syringate Degradation by Sphingomonas paucimobilis SYK-6

2005 ◽  
Vol 187 (15) ◽  
pp. 5067-5074 ◽  
Author(s):  
Daisuke Kasai ◽  
Eiji Masai ◽  
Keisuke Miyauchi ◽  
Yoshihiro Katayama ◽  
Masao Fukuda
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequences ◽  
Terminal Region ◽  
Ring Cleavage ◽  
Sphingomonas Paucimobilis ◽  
Acid Protein ◽  
Demethylation Pathway ◽  
Dioxygenase Gene ◽  
Amino Acid Protein

ABSTRACT Sphingomonas paucimobilis SYK-6 converts vanillate and syringate to protocatechuate (PCA) and 3-O-methylgallate (3MGA) in reactions with the tetrahydrofolate-dependent O-demethylases LigM and DesA, respectively. PCA is further degraded via the PCA 4,5-cleavage pathway, whereas 3MGA is metabolized via three distinct pathways in which PCA 4,5-dioxygenase (LigAB), 3MGA 3,4-dioxygenase (DesZ), and 3MGA O-demethylase (LigM) are involved. In the 3MGA O-demethylation pathway, LigM converts 3MGA to gallate, and the resulting gallate appears to be degraded by a dioxygenase other than LigAB or DesZ. Here, we isolated the gallate dioxygenase gene, desB, which encodes a 418-amino-acid protein with a molecular mass of 46,843 Da. The amino acid sequences of the N-terminal region (residues 1 to 285) and the C-terminal region (residues 286 to 418) of DesB exhibited ca. 40% and 27% identity with the sequences of the PCA 4,5-dioxygenase β and α subunits, respectively. DesB produced in Escherichia coli was purified and was estimated to be a homodimer (86 kDa). DesB specifically attacked gallate to generate 4-oxalomesaconate as the reaction product. The Km for gallate and the V max were determined to be 66.9 ± 9.3 μM and 42.7 ± 2.4 U/mg, respectively. On the basis of the analysis of various SYK-6 mutants lacking the genes involved in syringate degradation, we concluded that (i) all of the three-ring cleavage dioxygenases are involved in syringate catabolism, (ii) the pathway involving LigM and DesB plays an especially important role in the growth of SYK-6 on syringate, and (iii) DesB and LigAB are involved in gallate degradation.

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