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Cloning fact sheet

V A Kozlov, S P Sapozhnikov, A I Sheptuhina, A V Golenkov
Considered natural and experimental amyloidosis models in the existing theories context and known amyloidogenesis mechanisms. Available clinical and experimental observations indicate that the opinion of a fatal incurable amyloidosis wrong. It is shown that there is a significant amount of experimental easily replicable amyloidosis models, which may be used for practicing the treatment methods of this pathology. We offer an amyloidosis models classification: natural (animal models with generic amyloidosis), cell clones, artificial (infectious, protein, etc...
2015: Vestnik Rossiĭskoĭ Akademii Meditsinskikh Nauk
Liqin Du, Hui Yang, Yunlong Huo, Hang Wei, Yuanjin Xu, Yutuo Wei, Ribo Huang
Sucrose phosphorylase, an important enzyme mainly involved in the generic starch and sucrose pathways, has now caught the attention of researchers due to its transglycosylation activity. A novel sucrose phosphorylase, unspase, has been isolated, and its transglycosylation properties were characterized. Compared with Bisp, the sucrose phosphorylase from Bifidobacterium adolescentis, unspase had two deleted regions in its C: -terminal. These deleted regions were probably equivalent to the important five-stranded anti-parallel β-sheet domain in sucrose phosphorylase...
September 2012: World Journal of Microbiology & Biotechnology
Camila Matiollo, Javier Vernal, Gabriela Ecco, Jean Borges Bertoldo, Guilherme Razzera, Emanuel M de Souza, Fábio O Pedrosa, Hernán Terenzi
Transthyretin-related proteins (TRPs) constitute a family of proteins structurally related to transthyretin (TTR) and are found in a large range of bacterial, fungal, plant, invertebrate, and vertebrate species. However, it was recently recognized that both prokaryotic and eukaryotic members of this family are not functionally related to transthyretins. TRPs are in fact involved in the purine catabolic pathway and function as hydroxyisourate hydrolases. An open reading frame encoding a protein similar to the Escherichia coli TRP was identified in Herbaspirillum seropedicae genome (Hs_TRP)...
October 2, 2009: Biochemical and Biophysical Research Communications
Jon López-Llano, Susana Maldonado, Marta Bueno, Anabel Lostao, Maria Angeles-Jiménez, Mariá P Lillo, Javier Sancho
Flavodoxins are well known one-domain alpha/beta electron-transfer proteins that, according to the presence or absence of a approximately 20-residue loop splitting the fifth beta-strand of the central beta-sheet, have been classified in two groups: long and short-chain flavodoxins, respectively. Although the flavodoxins have been extensively used as models to study electron transfer, ligand binding, protein stability and folding issues, the role of the loop has not been investigated. We have constructed two shortened versions of the long-chain Anabaena flavodoxin in which the split beta-strand has been spliced to remove the original loop...
November 5, 2004: Journal of Biological Chemistry
Melva L Gonzalez, Mark Barton Frank, Paul A Ramsland, Jay S Hanas, Frank J Waxman
This study explores the structural features of murine monoclonal IgG2a anti-dinitrophenyl (DNP) antibodies that were previously shown to form immune complexes (IC) differing in their capacity to bind complement, their clearance from the circulation and their deposition in the kidney. Interestingly, the sequence of one of these antibodies has a missing stretch of 14 amino acids within FR3. Molecular modeling suggests that this sequence deletion corresponds to the loss of beta-pleated sheet structure for two beta-strands (designated 4-3 and 4-4) on the external surface of the V(H) domain...
October 2003: Molecular Immunology
Suzana Dos Reis, Bénédicte Coulary-Salin, Vincent Forge, Ioan Lascu, Joël Bégueret, Sven J Saupe
The HET-s protein of Podospora anserina is a fungal prion. This protein behaves as an infectious cytoplasmic element that is transmitted horizontally from one strain to another. Under the prion form, the HET-s protein forms aggregates in vivo. The specificity of this prion model compared with the yeast prions resides in the fact that under the prion form HET-s causes a growth inhibition and cell death reaction when co-expressed with the HET-S protein from which it differs by 13 residues. Herein we describe the purification and initial characterization of recombinant HET-s protein expressed in Escherichia coli...
February 22, 2002: Journal of Biological Chemistry
S M Lankford, S A Bai, J A Goldstein
Cytochrome P450 (CYP) 2E1 is a toxicologically important enzyme that inactivates a number of drugs and xenobiotics and also bioactivates many xenobiotic substrates to their hepatotoxic or carcinogenic forms. Although cDNAs for the human, rodent, and rabbit forms of CYP2E1 have been isolated and studied extensively, there is an absence of information about canine CYP2E1, despite the fact that the dog is routinely used in drug safety studies. In this study, we isolated and sequenced a full-length CYP2E1 cDNA from a beagle liver cDNA library...
August 2000: Drug Metabolism and Disposition: the Biological Fate of Chemicals
V O Lewis, M Gehrmann, L Weissbach, J E Hyman, A Rielly, D G Jones, M Llinás, J Schaller
The cDNA corresponding to exons 2-4 of the processed human plasminogen (Pgn) gene, encoding the N-terminal peptide domain (NTP), has been cloned, expressed in Escherichia coli as a recombinant protein (r-NTP) containing a hexahistidine tag, and refolded to the native structure that contains two internal cystine bridges. RNA expression of the two Pgn-related genes, PRG A and PRG B, that potentially encode 9-kDa polypeptides having extensive similarity to the NTP has been investigated. Using RNA-based PCR with liver RNA as template, we demonstrate that PRG A encodes a detectable mRNA species...
February 1999: European Journal of Biochemistry
S Ruvinov, L Wang, B Ruan, O Almog, G L Gilliland, E Eisenstein, P N Bryan
In complex with subtilisin BPN', the 77 amino acid prodomain folds into a stable compact structure comprising a four-stranded antiparallel beta-sheet and two three-turn alpha-helices. When isolated from subtilisin, the prodomain is 97% unfolded even under optimal folding conditions. Traditionally, to study stable proteins, denaturing cosolvents or temperatures are used to shift the equilibrium from folded to unfolded. Here we manipulate the folding equilibrium of the unstable prodomain by introducing stabilizing mutations generated by design...
August 26, 1997: Biochemistry
P R Young, D Sylvester
We have cloned the rabbit IL-1 beta cDNA, which encodes a 268 amino acid precursor similar in length to other sequenced IL-1 precursors. Comparison of all published IL-1 alpha and IL-1 beta sequences respectively indicates that the IL-1 alpha gene family is evolving faster than the IL-1 beta family, and that the two genes diverged approximately 270 million years ago. Surprisingly, there are differences in the regions preferentially conserved within the two families. The IL-1 alpha family is most conserved at the amino terminus whereas the IL-1 beta family is most conserved in the carboxy-terminal half...
May 1989: Protein Engineering
B Redl, P Holzfeind, F Lottspeich
The gene encoding human tear prealbumin, a major component of the protein fraction of tear fluid, was cloned from total cDNA of lacrimal gland by polymerase chain reaction using synthetic oligonucleotides derived from N-terminal amino acid sequences of the purified protein. Sequence analysis and a computer-assisted homology search revealed this protein to be a member of the lipocalin superfamily, consisting of hydrophobic-ligand carriers. The deduced amino acid sequence of tear prealbumin shares 58% identity with von Ebner's gland protein from rat, which is supposed to be involved in taste reception...
October 5, 1992: Journal of Biological Chemistry
R L Sheets, R Pandey, V Klement, C K Grant, P Roy-Burman
In efforts to elucidate the proximal leukemogens that might be produced during a feline leukemia virus (FeLV) infection of cats, homologous recombinations between molecularly cloned exogenous and endogenous FeLV proviruses of known sequences were examined in cell cultures in vitro. A plasmid containing an infectious member of the most commonly occurring FeLV subgroup (FeLV subgroup A or FeLV-A) was coexpressed with noninfectious constructs containing the envelope (env) gene of an endogenously inherited FeLV-like feline genomic element in transfected feline fibroblasts...
October 1992: Virology
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