Cloning, high-level gene expression and bioinformatics analysis of SP15 and LeIF from Leishmania major and Iranian Phlebotomus papatasi saliva as single and novel fusion proteins: a potential vaccine candidate against leishmaniasis.

Background: Early exacerbation of cutaneous leishmaniasis is mainly affected by both the salivary and Leishmania parasite components. Little is known of the vaccine combination made by immunogenic proteins of sandfly saliva (SP15) with Leishmania parasites (LeIF) as a single prophylactic vaccine, namely SaLeish. Also, there are no data available to determine the species-specific sequence of SP15 isolated from the Iranian Phlebotomus papatasi.

In silico design and analysis of a new hyperglycosylated analog of erythropoietin to improve drug efficacy.

Background: The enhancement of glycosylation by applying glycoengineering approaches has become widely used to boost properties for protein therapeutics. The objective of this work was to engineer a new hyperglycosylated analog of erythropoietin (EPO) with appropriately targeted N-linked carbohydrates through bioinformatics tools.

Materials And Methods: The EPO protein sequence was retrieved from NCBI protein sequence database.

Response surface methodology to optimize partition and purification of two recombinant oxidoreductase enzymes, glucose dehydrogenase and d-galactose dehydrogenase in aqueous two-phase systems.

Oxidoreductases are an important family of enzymes that are used in many biotechnological processes. An experimental design was applied to optimize partition and purification of two recombinant oxidoreductases, glucose dehydrogenase (GDH) from Bacillus subtilis and d-galactose dehydrogenase (GalDH) from Pseudomonas fluorescens AK92 in aqueous two-phase systems (ATPS). Response surface methodology (RSM) with a central composite rotatable design (CCRD) was performed to optimize critical factors like polyethylene glycol (PEG) concentration, concentration of salt and pH value.

Expression, Purification and Characterization of the Proline Dehydrogenase Domain of PutA from Pseudomonas putida POS-F84.

The objective of the present work was to express a truncated form of Pseudomonas putida PutA that shows proline dehydrogenase (ProDH) activity. The putA gene encoding ProDH enzyme was cloned into pET23a vector and expressed in Escherichia coli strain BL-21 (DE3) plysS. The recombinant P.

Polymorphism of the CLDN5 gene and Schizophrenia in an Iranian Population.

Background: The gene coding claudin (CLDN5) is located on 22q11. Since the proteins of CLDN5 family are a ma-jor component for barrier-forming tight junctions, it may be important to test whether or not the CLDN5 locus could be associated with schizophrenia.

Method: A total of 150 individuals affected with schizophrenia and 150 healthy persons were recruited.

Process integration for the recovery and purification of recombinant Pseudomonas fluorescens proline dehydrogenase using aqueous two-phase systems.

The integration of refolding, reconstitution and two-phase partitioning in aqueous two-phase systems (ATPS) which is composed of polyethylene glycol (PEG) and sodium carbonate (Na2CO3) was employed as a novel method for recovery and purification of recombinant Pseudomonas fluorescens proline dehydrogenase (ProDH). To obtain an optimal condition, the influence of different parameters, such as PEG molecular weight (MW), type and concentration of salt, pH, and NaCl addition on the partitioning features of target enzyme was also investigated. Combining the refolding, reconstitution and two-phase partitioning in an optimized ATPS of 14% (w/w) PEG-1000 and 12% (w/w) Na2CO3 at pH 8.

Rapid one-step separation and purification of recombinant phenylalanine dehydrogenase in aqueous two-phase systems.

Background: Phenylalanine dehydrogenase (PheDH; EC 1.4.1.

Preliminary report of NAD+-dependent amino acid dehydrogenase producing bacteria isolated from soil.

Background: Amino acid dehydrogenases (L-amino acid: oxidoreductase deaminating; EC 1.4.1.