Preferencje help
Polish version English version Język
Widoczny [Schowaj] Abstrakt
Liczba wyników

Znaleziono wyników: 7

Liczba wyników na stronie
Pierwsza strona wyników Pięć stron wyników wstecz Poprzednia strona wyników Strona / 1 Następna strona wyników Pięć stron wyników wprzód Ostatnia strona wyników

Wyniki wyszukiwania

Wyszukiwano:
w słowach kluczowych:  cDNA cloning
help Sortuj według:

help Ogranicz wyniki do:
Pierwsza strona wyników Pięć stron wyników wstecz Poprzednia strona wyników Strona / 1 Następna strona wyników Pięć stron wyników wprzód Ostatnia strona wyników
1

cDNA cloning, gene organization and expression analysis of human peptidylarginine deiminase type VI

100%
Zhang J., Dai J., Zhao E., Lin Y., Zeng L., Chen J., Zheng H., Wang Y., Li X., Ying K., Xie Y., Mao Y.
Acta Biochimica Polonica
|
2004
|
tom 51
|
nr 4
Peptidylarginine deiminase (PAD) catalyzes the post-translational modification of protein through the conversion of arginine to citrulline in the presence of calcium ions. Human, similar to rodents, has four isoforms of PAD (type I, II, III and IV/V), each of which is distinct in substrate specificity and tissue specific expression. In our large-scale sequencing project, we identified a new human PAD cDNA from a human fetal brain cDNA library. The putative protein encoded by this cDNA is designated hPADVI. Expression analysis of hPADVI showed that it is mainly expressed in adult human ovary and peripheral blood leukocytes. We conclude that hPADVI may be orthologous to mouse ePAD, basing on sequence comparison, chromosome localiza­tion and exon-intron structure analysis. PAD-mediated deimination of epithelial cell keratin resulting in cytoskeletal remodeling suggests a possible role for hPADVI in cytoskeletal reorganization in the egg and in early embryo development. This study describes a new important member of the human PAD family.
2

Cloning and characterisation of the 5'part of the high molecular weight transcript of rat DNA polymerase beta

100%
Konopinski R., Nowak R., Siedlecki J. A.
Acta Biochimica Polonica
|
1995
|
tom 42
|
nr 2
A rat brain cDNA library has been constructed. Three identical clones of about 2.2 kb representing high molecular weight DNA polymerase p transcript were found. Sequencing proved our earlier suggestion that both high and low molecular weight DNA polymerase p transcripts have the same open reading frame and differ mainly at the 3' end. Because of that, alternative polyadenylation is discussed as a possible mechanism for tissue- and development-specific regulation of the DNA polymerase p gene expression.
3

Ribosomal proteins L34 and S29 of amphioxus Branchiostoma belcheri tsingtauense: cDNAs cloning and gene copy number

86%
Liu L., Zhang S., Liu Z., Li H., Liu M., Wang Y., Ma L.
Acta Biochimica Polonica
|
2005
|
tom 52
|
nr 4
The complete cDNA and deduced amino-acid sequences of ribosomal proteins L34 (AmphiL34) and S29 (AmphiS29) from the amphioxus Branchiostoma belcheri tsingtauense were identified in this study. The AmphiL34 cDNA is 435 nucleotides in length and encodes a 118 amino-acid protein with calculated molecular mass of 13.6 kDa. It shares 53.6-67.5% amino-acid sequence identity with its eukaryotic counterparts including human, mouse, rat, pig, frog, catfish, fruit fly, mosquito, armyworm, nematode and yeast. The AmphiS29 cDNA comprises 453 nucleotides and codes for a 56 amino-acid protein with a calculated molecular mass of 6.6 kDa. It shows 66.1-78.6% amino-acid sequence identity to eukaryotic S29 proteins from human, mouse, rat, pig, zebrafish, seahorse, fruit fly, nematode, sea hare and yeast. AmphiL34 contains a putative nucleolar localization signal, while AmphiS29 has a zinc finger-like domain. A phylogenetic tree deduced from the conserved sequences of AmphiL34 and AmphiS29 and other known counterparts indicates that the positions of AmphiL34/AmphiS29 are intermediate between the vertebrate and invertebrate L34/S29. Southern blot analysis demonstrates the presence of one copy of the L34 gene and 2-3 copies of the S29 gene in the genome of the amphioxus B. belcheri tsingtauense. This is in sharp contrast to the existence of 7-9 copies of the L34 gene and 14-17 copies of the S29 gene in the rat genome. These date suggest that housekeeping genes like AmphiL34 and AmphiS29 have undergone large-scale duplication in the chordate lineage.
4

Molecular cloning and bioinformatic characterisation of FhPcW1, a new isoform of cathepsin L from adult Fasciola hepatica

72%
Jaros S., Zygner W., Januszkiewicz K., Jaros D., Wedrychowicz H.
Bulletin of the Veterinary Institute in Puławy
|
2010
|
tom 54
|
nr 4
The aim of this study was to clone new secretory antigen of Fasciola hepatica and to predict its availability for immune system. The new cathepsin L - FhPcW1 (F. hepatico cysteine proteinase Warsaw 1), GenBank accession: EF407948, cDNA was cloned from adult F. hepatica flukes using RACE-PCR method. FhPcW1 is encoded by a 1,066 bp mRNA with a predicted open reading frame (ORF) of 326 amino acids (predicted pl = 5.41, m.w. = 37.137 kDa). Performed bioinformatic analysis included alignments of the nucleotide and amino acid sequences, the ExPASy (Expert Protein Analysis System) proteomics server of the Swiss Institute of Bioinformatics and National Center for Biotechnology Information. Performed analyses allowed to suppose that FhPcW1 is a secreted protein, which contains signal peptide, serine, threonine, tyrosine phosphorylation sites and four tyrosine sulfation sites, and does not contain glycosylation sites. The ORF corresponding to FhPcW1 exhibited strong similarity to previously cloned cathepsins L from the F. hepatico as well as F. gigantica. Predicted biochemical characteristics fits to the described before F. hepatica cathepsin Ls. Moreover, three dimensional model and MHC types ligation strength prediction were performed. Analysis of MHC type I and II peptide binding suggests that FhPcW1 may have significant immunogenic potential. The potential HLA II epitopes are situated at the outer surface of this protein. Thus, these epitopes seems to be available for immune response, especially for antibodies. This result may show that FhPcW1 seems to be a promising antigen for vaccination against F. hepatica.
5

Cloning of the lymphoid enhancer binding factor-1 [Lef-1] cDNA from rat kidney: Homology to the mouse sequence

72%
Kobielak K., Kobielak A., Trzeciak W. H.
Acta Biochimica Polonica
|
1999
|
tom 46
|
nr 4
We have cloned and sequenced rat cDNA that encodes the Lef-1 protein. The cDNA, containing 1194 nt exhibits 94% similarity to the mouse Lef-1 cDNA. The deduced amino-acids sequence of rat Lef-1 protein, consisting of 397 amino acids, exhibited 98% homology with the known sequence of mouse Lef-1 protein.
6

Isolation of Nicotiana plumbaginifolia cDNAs encoding isoforms of serine acetyltransferase and O-acetylserine [thiol] lyase in a yeast two-hybrid system with Escherichia coli cysE and cysK genes as baits

58%
Liszewska F., Gaganidze D., Sirko A.
Acta Biochimica Polonica
|
2005
|
tom 52
|
nr 1
We applied the yeast two-hybrid system for screening of a cDNA library of Nicotiana plumbaginifolia for clones encoding plant proteins interacting with two proteins of Escherichia coli: serine acetyltransferase (SAT, the product of cysE gene) and O-acetylserine (thiol)lyase A, also termed cysteine synthase (OASTL-A, the product of cysK gene). Two plant cDNA clones were identified when using the cysE gene as a bait. These clones encode a probable cytosolic isoform of OASTL and an organellar isoform of SAT, respectively, as indicated by evolutionary trees. The second clone, encoding SAT, was identified independently also as a “prey” when using cysK as a bait. Our results reveal the possibility of applying the two-hybrid system for cloning of plant cDNAs encoding enzymes of the cysteine synthase complex in the two-hybrid system. Additionally, using genome walking sequences located upstream of the sat1 cDNA were identified. Subsequently, in silico analyses were performed aiming towards identification of the potential signal peptide and possible location of the deduced mature protein encoded by sat1.
7

Mouse cytosolic acetyl-CoA hydrolase, a novel candidate for a key enzyme involved in fat metabolisme: cDNA cloning sequencing and functional expression

58%
Suematsu N., Okamoto K., Isohashi F.
Acta Biochimica Polonica
|
2002
|
tom 49
|
nr 4
A cytosolic acetyl-CoA hydrolase (CACH) cDNA has been isolated from mouse liver cDNA library and sequenced. Recombinant expression of the cDNA in insect cells re­sulted in overproduction of active acetyl-CoA hydrolyzing enzyme protein. The mouse CACH cDNA encoded a 556-amino-acid sequence that was 93.5% identical to rat CACH, suggesting a conserved role for this enzyme in the mammalian liver. Database searching shows no homology to other known proteins, but reveals homological cDNA sequences showing two single-nucleotide polymorphisms (SNPs) in the CACH coding region. The discovery of mouse CACH cDNA is an important step towards genetic studies on the functional analysis of this enzyme by gene-knockout and transgenic ap­proaches.
Pierwsza strona wyników Pięć stron wyników wstecz Poprzednia strona wyników Strona / 1 Następna strona wyników Pięć stron wyników wprzód Ostatnia strona wyników
JavaScript jest wyłączony w Twojej przeglądarce internetowej. Włącz go, a następnie odśwież stronę, aby móc w pełni z niej korzystać.