cDNA Cloning of the hydroxysteroid sulfotransferase STa sharing a strong homology in amino acid sequence with the senescence marker protein SMP-2 in rat livers

1990 ◽  
Vol 166 (3) ◽  
pp. 1494-1500 ◽  
Author(s):  
Kenichiro Ogura ◽  
Jiro Kajita ◽  
Hiroyuki Narihata ◽  
Tadashi Watabe ◽  
Shogo Ozawa ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Cdna Cloning ◽  
Marker Protein ◽  
Strong Homology ◽  
Rat Livers

Amino acid sequence of a unique neuronal protein: Rat olfactory marker protein

1986 ◽  
Vol 249 (2) ◽  
pp. 351-362 ◽  
Author(s):  
W. Sydor ◽  
Z. Teitelbaum ◽  
R. Blacher ◽  
S. Sun ◽  
W. Benz ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Marker Protein ◽  
Olfactory Marker Protein ◽  
Neuronal Protein

scholarly journals Purification from Placenta, Amino Acid Sequence, Structure Comparisons and cDNA Cloning of Human Glutaredoxin

1995 ◽  
Vol 227 (1-2) ◽  
pp. 27-34 ◽  
Author(s):  
C. Alicia Padilla ◽  
Emilia Martinez-Galisteo ◽  
J. Antonio Barcena ◽  
Giannis Spyrou ◽  
Arne Holmgren
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Cdna Cloning ◽  
Sequence Structure

Identification and cDNA cloning of a Xenopus nucleolar phosphoprotein, xNopp180, that is the homolog of the rat nucleolar protein Nopp140

1995 ◽  
Vol 108 (10) ◽  
pp. 3339-3347 ◽  
Author(s):  
C. Cairns ◽  
B. McStay
Keyword(s):  
Monoclonal Antibody ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Cdna Cloning ◽  
Cdna Clone ◽  
Xenopus Oocyte ◽  
Ribosome Biogenesis ◽  
Nucleolar Protein ◽  
Nuclear Localisation Signal ◽  
Cdc2 Kinase

The monoclonal antibody G1C7, recognises both Xenopus nucleolin and a protein of 180 kDa present in Xenopus oocyte nucleoli. This antibody was used to obtain a cDNA clone encoding the 180 kDa protein now called xNopp180 (Xenopus nucleolar phosphoprotein of 180 kDa). Analysis of the deduced amino acid sequence from this cDNA shows that xNopp180 is almost entirely composed of alternating acidic and basic domains. We show that xNopp180 is heavily phosphorylated and that it contains multiple consensus sites for phosphorylation by casein kinase II and cdc2 kinase. In addition we show that xNopp180 is the 180 kDa antigen recognised by the monoclonal antibody No-114, thus allowing reinterpretation of previous work with this antibody. xNopp180 appears to be the Xenopus homolog of the rat nucleolar protein Nopp140. Nopp140 is a nuclear localisation signal binding protein that shuttles on curvilinear tracks between the nucleolus and the cytoplasm. Possible roles for xNopp180/Nopp140 in ribosome biogenesis are discussed.

scholarly journals Cloning and characterization of a second member of the mouse mdr gene family.

1988 ◽  
Vol 8 (7) ◽  
pp. 2770-2778 ◽  
Author(s):  
P Gros ◽  
M Raymond ◽  
J Bell ◽  
D Housman
Keyword(s):  
Multidrug Resistance ◽  
Amino Acid ◽  
Nucleotide Sequence ◽  
Amino Acid Sequence ◽  
Gene Family ◽  
Predicted Amino Acid Sequence ◽  
Coding Region ◽  
Physiological Processes ◽  
Strong Homology ◽  
Energy Dependent

The mammalian mdr gene family comprises a small number of closely related genes. Previously, we have shown that one member, mdr1, has the capacity to convey multidrug resistance to drug-sensitive recipient cells in a gene transfer protocol. However, the functional characteristics of other members of this gene family have not been examined. In this report, we characterize a second member of the mdr gene family which we designated mdr2. We determined the nucleotide sequence corresponding to the complete coding region of this mdr2 transcript. The predicted amino acid sequence of this protein (1,276 amino acids) showed that it is a membrane glycoprotein highly homologous to mdr1 (85%), strongly suggesting that both genes originate from a common ancestor. Regions of divergence between mdr1 and mdr2 proteins are concentrated in two discrete segments of the predicted polypeptides, each approximately 100 residues in length. The mdr2 protein appears to be formed by the duplication of a structural unit which encodes three putative transmembrane loops and a predicted nucleotide-binding fold and is highly homologous to bacterial transport proteins such as hlyB. This strong homology suggests that mdr2 also participates in an energy-dependent membrane transport process. However, the direct relationship, if any, of this new member of the mdr family to multidrug resistance remains to be established. Knowledge of the complete nucleotide sequence and predicted amino acid sequence of the mdr2 gene product will enable the preparation of gene-specific probes and antibodies necessary to study the functional role of this gene in multidrug resistance and normal physiological processes.

scholarly journals Amino acid sequence of Fel dI, the major allergen of the domestic cat: protein sequence analysis and cDNA cloning.

1991 ◽  
Vol 88 (21) ◽  
pp. 9690-9694 ◽  
Author(s):  
J. P. Morgenstern ◽  
I. J. Griffith ◽  
A. W. Brauer ◽  
B. L. Rogers ◽  
J. F. Bond ◽  
...  
Keyword(s):  
Amino Acid ◽  
Sequence Analysis ◽  
Amino Acid Sequence ◽  
Cdna Cloning ◽  
Protein Sequence ◽  
Major Allergen ◽  
Domestic Cat ◽  
Protein Sequence Analysis
Sign in / Sign up

Export Citation Format

Share Document