Screening of phage-displayed human liver cDNA library against doxorubicin with drug-immobilized monolithic polyacrylamide cryogel

2013 ◽  
Vol 27 (11) ◽  
pp. 1574-1579 ◽  
Author(s):  
Xiaoming Yu ◽  
Peng Zhao ◽  
Lihua Zhang ◽  
Yukui Zhang



2007 ◽  
Vol 45 (5) ◽  
pp. 701-705 ◽  
Author(s):  
Xiaoming Yu ◽  
Peng Zhao ◽  
Weibing Zhang ◽  
Lihua Zhang ◽  
Yukui Zhang


1987 ◽  
Author(s):  
J K Ploos van Amstel ◽  
A L van der Zanden ◽  
E Bakker ◽  
P H Reitsma ◽  
R M Bertina

Protein S is a vitamin K-dependent glycoprotein, that serves as a cofactor of activated protein C. A hereditary deficiency in protein S is associated with an increased risk for the development of venous thrombosis. The deficiency is inherited as an autosomal dominant trait. We isolated a cDNA coding for protein S and assigned its gene to chromosome 3.A human liver cDNA library in phage xgtll (complexity 1.2 × 106 , D. Stafford, Chapel Hill) was screened by using immuno-purifiedpolyclonal anti-protein S IgG as a probe. Approximately 1.5 x 10 recombinants of the amplified library were screened. Out of eighteen positive clones one clone was found, after nucleotide sequence analysis, to code for a peptide with a high degree of homology with the carboxy terminal region of the already published bovine protein S. This clone pSP84 (450 bp) was used as a probe to screen a human liver cDNA library in plasmid pUC9. From this library we isolated several positive clones. Clone pSUL5 contained the largest insert (2200 base pairs). Dideoxy sequencing revealed that it codes for 330 amino acids of the carboxy terminal part of protein S. Furthermore, it contained a 1200 base pairs 3' untranslated region. The predicted amino acid sequence did not differ from the published sequence of human protein S, although at the nucleotide level some differences could be detected.Clone pSUL5 was used to localize the protein S gene to its chromosome. The assignment was done by hybridization to Pst I digested DNA from human-hamster c.q. human-mouse somatic cell hybrids. In this way we got strong indication that the protein S gene is located on chromosome 3.





2012 ◽  
Vol 39 (8) ◽  
pp. 8225-8230 ◽  
Author(s):  
Xiaolan Li ◽  
Xuelai Luo ◽  
Zhaoming Li ◽  
Guihua Wang ◽  
Hui Xiao ◽  
...  


1993 ◽  
Vol 289 (1) ◽  
pp. 233-240 ◽  
Author(s):  
K A Comer ◽  
J L Falany ◽  
C N Falany

Dehydroepiandrosterone sulphotransferase (DHEA-ST) catalyses the 3′-phosphoadenosine 5′-phosphosulphate-dependent sulphation of a wide variety of steroids in human liver and adrenal tissue and is responsible for most, if not all, of the sulphation of bile acids in human liver. This report describes the isolation, characterization and expression of a cDNA which encodes human liver DHEA-ST. The DHEA-ST cDNA, designated DHEA-ST8, was isolated from a Uni-Zap XR human liver cDNA library and is composed of 1060 bp and contains an open reading frame encoding a 285-amino-acid protein with a molecular mass of approx. 33765 Da. Translation of DHEA-ST8 in vitro generated a protein identical in molecular size with that of DHEA-ST. Expression of DHEA-ST8 in COS-7 cells produces an active DHEA-ST protein which is capable of sulphating DHEA, has the same molecular mass as human liver DHEA-ST and is recognized by rabbit anti-(human liver DHEA-ST) antibodies. Northern-blot analysis of human liver RNA detects the presence of three different size transcripts; however, Southern-blot analysis of human DNA suggests that only one gene may be present in the genome. These results describe the cloning of a human ST which has an important role in the sulphation of steroids and bile acids in human liver and adrenals.



1995 ◽  
Vol 213 (1) ◽  
pp. 154-160 ◽  
Author(s):  
C.H. Baker ◽  
S.P.T. Matsuda ◽  
D.R. Liu ◽  
E.J. Corey


FEBS Letters ◽  
1986 ◽  
Vol 196 (1) ◽  
pp. 108-112 ◽  
Author(s):  
Y. Le Bouc ◽  
D. Dreyer ◽  
F. Jaeger ◽  
M. Binoux ◽  
P. Sondermeyer


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