Abstract: The present invention relates to a chromatographic process for obtaining purified fibrinogen and thrombin from human plasma. The purified fibrinogen and thrombin preparations contain plasminogen in amounts less than 1 ug/mL. The low levels of plasminogen eliminates use of a proteolytic inhibitor, such as aprotinin in fibrin sealant kits which are used for human therapeutic applications.

Abstract: The invention is an integrated process for the isolation and purification of plasma derived clotting Factor VIII, clotting Factor IX, albumin and immunoglobulin without the use of ethanol precipitation. The integrated process comprises of sequential chromatography steps of gel filtration, anion exchange and cation exchange chromatographies, followed by viral inactivation and removal steps. The present invention has the advantage of being a mild process that does not denature or aggregate the proteins and provides high yields of several therapeutic grade plasma proteins from a given volume of plasma.

Abstract: The present invention relates to a fibrin sealant kit comprising purified fibrinogen and thrombin. The invention particularly relates to an improved chromatographic process for the purification of thrombin and fibrinogen components devoid of any significant plasminogen and other impurities. The absence of plasminogen facilitates the exclusion of a proteolytic inhibitor (aprotinin) from among the kit components.

Abstract: The invention relates to an integrated scheme for fractionation and purification of plasma products (human albumin, intravenous immunoglobulin (IVIG), clotting factor VIII and clotting factor IX) by sequential chromatography and virus reduction steps. The therapeutically administrable protein IVIG has purity levels exceeding 98%, aggregates and dimers at less than 0.2%, Fc function of >90% and anti-complementary activity of less than 0.5 CH50 per mg of Ig. The distribution of IgG isomers is comparable to the ranges seen in normal plasma. Human albumin for therapeutic use, purified by this integrated scheme has an electrophoretic purity of close to 100%, with monomers exceeding 98%. The levels of aluminium and pre-kallikrein activator are below the detection limit for the respective tests. The Factor IX preparations have a specific activity of ?200 IU/mg. The impurity levels of Factor-II, Factor VII, Factor X are at least 10-fold lesser (?0.5% instead of 5%) and the heparin impurity of ?0.01 IU (against 0.

Abstract: The use of a tag moiety comprising a biotinylation domain, such as biotin carboxyl carrier protein (BCCP), as a protein folding marker and protein solubility enhancer in the orientated surface capture of products of heterologously expressed genes is described. Methods for increasing the solubility of proteins and determining the folded state of a protein are also disclosed. The uses and methods of the invention can be carried out in a multiplexed manner on more than one protein in the formation of libraries. In addition the nucleic acid molecule encoding the biotinylation domain of the tag moiety can be used to increase the proportion of clones in a library that express the protein of interest.

Abstract: The present invention describes methods for the preparation of protein arrays of full length proteins. The use of such arrays in screening methods is also described.

Abstract: The present invention provides a method for achieving high-level expression of the therapeutically important lymphokine (human IL-2). The method comprises of identifying the secondary structure in the 5? region of human IL-2 mRNA, modifying the 5? region of the human IL-2 DNA sequence to produce a new DNA sequence wherein the mRNA transcribed from the modified human IL-2 DNA sequence has the predicted 5? secondary structure destabilized with increased free energy compared to that of the secondary structure of the mRNA transcribed from the native DNA sequence without altering the sequence of the encoded amino acids; and using this modified DNA sequence of human IL-2 for high level recombinant expression in a microbial host for large scale production. This method is also applicable to other expression host like yeasts and mammalian cells.

Abstract: The present invention describes a novel process for large scale purification of therapeutic grade quality of recombinant human G-CSF from microbial cells, wherein the protein is expressed as inclusion bodies. The process involves the novel use of Hydrophobic Interaction Chromatography (HIC) step to purify G-CSF eluted from a cation exchange column. A combination of these two chromatography steps provides good purity and yields which are essential for a production scale process. The host cell related contaminants like proteins, DNA and endotoxins are estimated to be within the specifications outlined by the drug regulatory authorities.

Abstract: The present invention relates to novel methods of producing proteins in which one or more domains are full length and correctly folded and which are each tagged at either the N- or C-terminus with one or more marker moieties and arrays containing such proteins, as well as the use of such proteins in arrays for rapid screening.

Abstract: The present invention relates to novel methods of producing proteins in which one or more domains are full length and correctly folded and which are each tagged at either the N— or C-terminus with one or more marker moieties and arrays containing such proteins, as well as the use of such proteins in arrays for rapid screening.

Abstract: The use of a tag moiety comprising a biotinylation domain, such as biotin carboxyl carrier protein (BCCP), as a protein folding marker and protein solubility enhancer in the orientated surface capture of products of heterologously expressed genes is described. Methods for increasing the solubility of proteins and determining the folded state of a protein are also disclosed. The uses and methods of the invention can be carried out in a multiplexed manner on more than one protein in the formation of libraries. In addition the nucleic acid molecule encoding the biotinylation domain of the tag moiety can be used to increase the proportion of clones in a library that express the protein of interest.

Abstract: The present invention describes methods for the preparation of protein arrays of full length proteins. The use of such arrays in screening methods is also described.

Abstract: The present invention relates to novel methods of producing proteins in which one or more domains are full length and correctly folded and which are each tagged at either the N- or C-terminus with one or more marker moieties and arrays containing such proteins, as well as the use of such proteins in arrays for rapid screening.