129 research outputs found
ΠΠ²ΡΠΎΠΌΠ°ΡΠΈΡΠ΅ΡΠΊΠ°Ρ ΠΎΠΏΡΠΈΠΌΠΈΠ·Π°ΡΠΈΡ ΡΠ΅Ρ Π½ΠΎΠ»ΠΎΠ³ΠΈΡΠ΅ΡΠΊΠΎΠ³ΠΎ ΠΊΠΎΠΌΠΏΠ»Π΅ΠΊΡΠ° ΠΎΠ±ΠΎΠ³Π°ΡΠ΅Π½ΠΈΡ ΠΆΠ΅Π»Π΅Π·Π½ΡΡ ΡΡΠ΄ ΠΏΠΎ ΡΠΈΠ³Π½Π°Π»Π°ΠΌ ΠΌΠ°Π³Π½ΠΈΡΠ½ΠΎΠΉ ΠΈΠ½Π΄ΡΠΊΡΠΈΠΈ ΡΠ΅ΠΏΠ°ΡΠ°ΡΠΎΡΠ°
Recombinant antibodies can be used to diagnose, treat and prevent disease by exploiting their specific antigen-binding activities. A large number of drugs currently in development are recombinant antibodies and most of these are produced in cultured rodent cells. Although such cells produce authentic functional products, they are expensive, difficult to scale-up and may contain human pathogens. Plants represent a cost-effective, convenient and safe alternative production system and are slowly gaining acceptance. Five plant-derived therapeutic recombinant antibodies (plantibodies) are undergoing clinical evaluation, three of which can be used as prophylactics
Molecular farming of human tissue transglutaminase in tobacco plants
In this study we have utilized Nicotiana tabacum with a molecular farming purpose in attempt of producing transgenic plants expressing the human tissue transglutaminase (htTG). Three plant expression constructs were used enabling targeting and accumulation of the recombinant protein into the plant cell cytosol (cyto), the chloroplasts (chl) and the apoplastic space (apo). Analysis of transgenic T(0) plants revealed that recombinant htTG was detectable in all three transgenic lines and the accumulation levels were in a range of 18-75 mu g/g of leaf material. In the T(1) generation, the recombinant htTG was still expressed at high level and a significant catalytic activity was detected into the leaf protein extracts. Southern blot analyses revealed that apo and chl plants of T(1) generation possess a high copy number of the recombinant htTG in their genome, while the cyto plants carry a single copy
ΠΡΠ°Π²ΠΎΠ²Ρ Π·Π°ΡΠ°Π΄ΠΈ Π·Π΄ΡΠΉΡΠ½Π΅Π½Π½Ρ Π΄ΡΡΠ»ΡΠ½ΠΎΡΡΡ Π·Ρ ΡΠΏΡΠ»ΡΠ½ΠΎΠ³ΠΎ ΡΠ½Π²Π΅ΡΡΡΠ²Π°Π½Π½Ρ
We describe the expression of the bispecific antibody biscFv2429 in transgenic suspension culture cells and tobacco plants. biscFv2429 consists of two single chain antibodies, scFv24 and scFv29, connected by the Trichoderma reesi cellobiohydrolase I linker. biscFv2429 binds two epitopes of tobacco mosaic virus (TMV): the scFv24 domain recognizes neotopes of intact virions, and the scFv29 domain recognizes a cryptotope of the TMV coat protein monomer. biscFv2429 was functionally expressed either in the cytosol (biscFv2429-cyt) or targeted to the apoplast using a murine leader peptide sequence (biscFv2429-apoplast). A third construct contained the C-terminal KDEL sequence for retention in the ER (biscFv2429-KDEL). Levels of cytoplasmic biscFv2429 expression levels were low. The highest levels of antibody expression were for apoplast targeted biscFv2429-apoplast and ER retained biscFv2429-KDEL, which reached a maximum expression level of 1.65% total soluble protein in transgenic plants. P lant expressed biscFv2429 retained both epitope specificities, and bispecificity and bivalency were confirmed by ELISA and surface plasmon resonance analysis. This study establishes plant cells as an expression system for bispecific single chain antibodies for use in medical and biological applications
Π‘Π²ΡΠ·Ρ ΠΌΠΈΠΊΡΠΎΡΠ»Π΅ΠΌΠ΅Π½ΡΠ½ΠΎΠ³ΠΎ ΡΠΎΡΡΠ°Π²Π° Spirodela polyrhiza (L.) Schleid ΡΠΎ ΡΡΠ΅Π΄ΠΎΠΉ Π΅Π³ΠΎ ΠΎΠ±ΠΈΡΠ°Π½ΠΈΡ
Plants and plant cell cultures have been evaluated over the past two decades as alternative production platforms for biopharmaceuticals. A large number of candidate proteins has been successfully produced in a range of plant species and the most advanced products are currently progressing through the clinical development stages. We first discuss principles for the production of plant-made pharmaceuticals including plant transformation procedures, post-translational modifications, and downstream processing. We then highlight some of the most advanced plant-made biopharmaceuticals currently in clinical development for human medical use
Π‘ΠΎΠ·Π΄Π°Π½ΠΈΠ΅ ΠΏΠΎΠ»ΠΈΠΌΠ΅ΡΠ½ΡΡ ΠΊΠΎΠΌΠΏΠΎΠ·ΠΈΡΠΈΠΎΠ½Π½ΡΡ ΠΌΠ°ΡΠ΅ΡΠΈΠ°Π»ΠΎΠ² Ρ Π½Π΅ΠΏΡΠ΅ΡΡΠ²Π½ΡΠΌ Π°ΡΠΌΠΈΡΠΎΠ²Π°Π½ΠΈΠ΅ΠΌ Π°ΡΠ°ΠΌΠΈΠ΄Π½ΡΠΌ Π²ΠΎΠ»ΠΎΠΊΠ½ΠΎΠΌ Π΄Π»Ρ ΠΏΡΠΈΠΌΠ΅Π½Π΅Π½ΠΈΡ Π² Π°Π΄Π΄ΠΈΡΠΈΠ²Π½ΡΡ ΡΠ΅Ρ Π½ΠΎΠ»ΠΎΠ³ΠΈΡΡ
Π Π΄Π°Π½Π½ΠΎΠΉ ΡΠ°Π±ΠΎΡΠ΅ ΠΏΡΠΎΠ²Π΅Π΄Π΅Π½ΠΎ ΠΈΡΡΠ»Π΅Π΄ΠΎΠ²Π°Π½ΠΈΠ΅ ΡΠΎΠ·Π΄Π°Π½ΠΈΡ ΠΊΠΎΠΌΠΏΠΎΠ·ΠΈΡΠΈΠΎΠ½Π½ΠΎΠ³ΠΎ ΠΌΠ°ΡΠ΅ΡΠΈΠ°Π»Π° Π½Π° ΠΏΠΎΠ»ΠΈΠΌΠ΅ΡΠ½ΠΎΠΉ ΠΎΡΠ½ΠΎΠ²Π΅ Ρ Π½Π΅ΠΏΡΠ΅ΡΡΠ²Π½ΡΠΌ Π°ΡΠΌΠΈΡΠΎΠ²Π°Π½ΠΈΠ΅ΠΌ Π°ΡΠ°ΠΌΠΈΠ΄Π½ΠΎΠ³ΠΎ Π²ΠΎΠ»ΠΎΠΊΠ½Π° Π΄Π»Ρ ΠΏΡΠΈΠΌΠ΅Π½Π΅Π½ΠΈΡ Π² Π°Π΄Π΄ΠΈΡΠΈΠ²Π½ΡΡ
ΡΠ΅Ρ
Π½ΠΎΠ»ΠΎΠ³ΠΈΡΡ
. ΠΠΏΠΈΡΠ°Π½Ρ ΡΠ΅Ρ
Π½ΠΎΠ»ΠΎΠ³ΠΈΡΠ΅ΡΠΊΠΈΠ΅ ΠΎΡΠΎΠ±Π΅Π½Π½ΠΎΡΡΠΈ ΠΏΡΠΎΡΠ΅ΡΡΠ° ΠΌΠΎΠ΄ΠΈΡΠΈΠΊΠ°ΡΠΈΠΈ ΠΏΠΎΠ²Π΅ΡΡ
Π½ΠΎΡΡΠΈ Π°ΡΠ°ΠΌΠΈΠ΄Π½ΠΎΠ³ΠΎ Π²ΠΎΠ»ΠΎΠΊΠ½Π°. ΠΡΡΠ»Π΅Π΄ΠΎΠ²Π°Π½ΠΎ Π²Π»ΠΈΡΠ½ΠΈΠ΅ ΠΌΠ°ΡΠ΅ΡΠΈΠ°Π»Π° ΠΌΠΎΠ΄ΠΈΡΠΈΠΊΠ°ΡΠΈΠΈ ΠΏΠΎΠ²Π΅ΡΡ
Π½ΠΎΡΡΠΈ Π½Π° Π°Π΄Π³Π΅Π·ΠΈΠΎΠ½Π½ΡΠ΅ ΡΠ²ΠΎΠΉΡΡΠ²Π° ΠΏΠΎΠ»ΡΡΠ°Π΅ΠΌΠΎΠ³ΠΎ ΠΊΠΎΠΌΠΏΠΎΠ·ΠΈΡΠΈΠΎΠ½Π½ΠΎΠ³ΠΎ ΠΌΠ°ΡΠ΅ΡΠΈΠ°Π»Π°
ΠΠ½Π°Π»ΠΈΠ· ΡΡΡΠ΅ΠΊΡΠΈΠ²Π½ΠΎΡΡΠΈ ΠΏΡΠΎΠ²Π΅Π΄Π΅Π½ΠΈΡ ΡΠΎΠ»ΡΠ½ΠΊΠΈΡΠ»ΠΎΡΠ½ΠΎΠΉ ΠΎΠ±ΡΠ°Π±ΠΎΡΠΊΠΈ Π½Π° ΠΊΠ°ΡΠ±Π½Π°ΡΠ½ΡΡ ΠΎΡΠ»ΠΎΠΆΠ΅Π½ΠΈΡΡ
Π Π°Π·ΡΠ°Π±ΠΎΡΠΊΠ° ΠΌΠ°ΡΠ΅ΠΌΠ°ΡΠΈΡΠ΅ΡΠΊΠΎΠΉ ΠΌΠΎΠ΄Π΅Π»ΠΈ ΠΏΡΠΎΡΠ΅ΡΡΠ° Π³ΠΈΠ΄ΡΠΎΠΎΡΠΈΡΡΠΊΠΈ Π²Π°ΠΊΡΡΠΌΠ½ΠΎΠ³ΠΎ Π΄ΠΈΡΡΠΈΠ»Π»ΡΡΠ°
Plants are now gaining widespread acceptance as a general platform for the large-scale production of recombinant proteins. The first plant-derived recombinant pharmaceutical proteins are reaching the final stages of clinical evaluation, and many more are in the development pipeline. Over the past two years, there have been some notable technological advances in this flourishing area of applied biotechnology, as shown by the continuing commercial development of novel plant-based expression platforms. There has also been significant success in tackling some of the limitations of plant bioreactors, such as low yields and inconsistent product quality, that have limited the approval of plant-derived pharmaceuticals
ΠΡΠ΅Π½ΠΊΠ° Π²ΠΎΠ·ΠΌΠΎΠΆΠ½ΠΎΡΡΠΈ ΠΌΠ΅ΡΠΎΠ΄Π° ΠΠΠΠΎΠ² Π΄Π»Ρ ΡΠ΅ΡΠ΅Π½ΠΈΡ Ρ Π°ΡΠ°ΠΊΡΠ΅ΡΠ½ΡΡ Π·Π°Π΄Π°Ρ ΠΏΠΎ ΠΈΠ·ΠΌΠ΅Π½Π΅Π½ΠΈΡ ΡΡΡΡΠΊΡΡΡΡ ΠΈ ΠΏΠ°ΡΠ°ΠΌΠ΅ΡΡΠΎΠ² ΡΠ΅ΠΏΠ»ΠΎΠ²ΡΡ ΡΡ Π΅ΠΌ ΠΠ’Π£ ΠΠΠ‘
ΠΠ±ΡΠ΅ΠΊΡΠΎΠΌ ΠΈΡΡΠ»Π΅Π΄ΠΎΠ²Π°Π½ΠΈΡ Π΄ΠΈΠΏΠ»ΠΎΠΌΠ½ΠΎΠΉ ΡΠ°Π±ΠΎΡΡ ΡΠ²Π»ΡΡΡΡΡ ΡΠΊΡΠΏΡΠ΅ΡΡ-ΠΌΠ΅ΡΠΎΠ΄Ρ ΡΠ΅ΡΠ΅Π½ΠΈΡ Ρ
Π°ΡΠ°ΠΊΡΠ΅ΡΠ½ΡΡ
Π·Π°Π΄Π°Ρ ΠΏΠΎ ΠΈΠ·ΠΌΠ΅Π½Π΅Π½ΠΈΡ ΡΡΡΡΠΊΡΡΡΡ ΡΠ΅ΠΏΠ»ΠΎΠ²ΡΡ
ΡΡ
Π΅ΠΌ ΠΠ’Π£ ΠΠΠ‘. Π¦Π΅Π»ΡΡ ΡΠ°Π±ΠΎΡΡ ΡΠ²Π»ΡΠ΅ΡΡΡ Π²ΡΡΠ²Π»Π΅Π½ΠΈΠ΅ ΡΡΠ°Π²Π½ΠΈΡΠ΅Π»ΡΠ½ΠΎΠΉ ΠΎΡΠ΅Π½ΠΊΠΈ ΡΠ΅Π·ΡΠ»ΡΡΠ°ΡΠΎΠ² ΡΠ°ΡΡΠ΅ΡΠΎΠ² ΡΠ΅ΠΏΠ»ΠΎΠ²ΡΡ
ΡΡ
Π΅ΠΌ ΡΠΊΡΠΏΡΠ΅ΡΡ-ΠΌΠ΅ΡΠΎΠ΄Π°ΠΌΠΈ. ΠΡΠΎΠ²ΠΎΠ΄ΠΈΠ»ΠΈΡΡ Π²Π°ΡΠΈΠ°Π½ΡΠ½ΡΠ΅ ΡΡΠ°Π²Π½ΠΈΡΠ΅Π»ΡΠ½ΡΠ΅ ΡΠ°ΡΡΠ΅ΡΡ ΠΏΡΠΈ ΠΈΠ·ΠΌΠ΅Π½Π΅Π½ΠΈΠΈ ΡΡΡΡΠΊΡΡΡΡ ΠΈ ΠΏΠ°ΡΠ°ΠΌΠ΅ΡΡΠΎΠ² ΡΠ΅ΠΏΠ»ΠΎΠ²ΡΡ
ΡΡ
Π΅ΠΌ.The object of the research thesis are rapid methods for solving specific problems of restructuring the thermal circuit Vocational plant. The aim is to identify the comparative evaluation of results of calculations of thermal schemes express methods. Were variant comparative calculations when changing the structure and parameters of thermal schemes
ΠΡΠΈΠΌΠ΅Π½Π΅Π½ΠΈΠ΅ Π±ΡΡΠΎΠ²ΡΡ ΡΠ»Π°ΠΌΠΎΠ² Π² ΠΈΠ·Π³ΠΎΡΠΎΠ²Π»Π΅Π½ΠΈΠΈ ΡΡΡΠΎΠΈΡΠ΅Π»ΡΠ½ΡΡ ΠΌΠ°ΡΠ΅ΡΠΈΠ°Π»ΠΎΠ²
Thrombomodulin is a membrane-bound protein that plays an active role in the blood coagulation system by binding thrombin and initiating the protein C anticoagulant pathway. Solulin (TM) is a recombinant soluble derivative of human thrombomodulin. It is used for the treatment of thrombotic disorders. To evaluate the production of this pharmaceutical protein in plants, expression vectors were generated using four different N-terminal signal peptides. Immunoblot analysis of transiently transformed tobacco leaves showed that intact Solulin (TM) could be detected using three of these signal peptides. Furthermore transgenic tobacco plants and BY2 cells producing Solulin (TM) were generated. Immunoblot experiments showed that Solulin (TM) accumulated to maximum levels of 115 and 27 mu g g(-1)supercript stop plant material in tobacco plants and BY2 cells, respectively. Activity tests performed on the culture supernatant of transformed BY2 cells showed that the secreted Solulin (TM) was functional. In contrast, thrombomodulin activity was not detected in total soluble protein extracts from BY2 cells, probably due to inhibitory effects of substances in the cell extract. N-terminal sequencing was carried out on partially purified Solulin (TM) from the BY2 culture supernatant. The sequence was identical to that of Solulin (TM) produced in Chinese hamster ovary cells, confirming correct processing of the N-terminal signal peptide. We have demonstrated that plants and plant cell cultures can be used as alternative systems for the production of an active recombinant thrombomodulin derivative
ΠΠ΅Π½Π½ΠΎΠ΅ ΠΏΠΎΠΆΠ°ΡΠΎΡΡΡΠ΅Π½ΠΈΠ΅: ΠΎΡΠΎΠ±Π΅Π½Π½ΠΎΡΡΠΈ Π² ΡΠΎΠ²ΡΠ΅ΠΌΠ΅Π½Π½ΡΡ ΡΡΠ»ΠΎΠ²ΠΈΡΡ
Π ΡΡΠ°ΡΡΠ΅ ΠΏΠΎΠΊΠ°Π·Π°Π½Ρ ΠΏΡΠ΅ΠΈΠΌΡΡΠ΅ΡΡΠ²Π° ΡΠΈΡΡΠ΅ΠΌ ΠΏΠ΅Π½Π½ΠΎΠ³ΠΎ ΠΏΠΎΠΆΠ°ΡΠΎΡΡΡΠ΅Π½ΠΈΡ. Π Π°ΡΡΠΌΠΎΡΡΠ΅Π½Ρ ΡΠΎΠ²ΡΠ΅ΠΌΠ΅Π½Π½ΡΠ΅ ΡΠ΅Π½Π΄Π΅Π½ΡΠΈΠΈ Π² ΠΏΠ΅Π½Π½ΠΎΠΌ ΠΏΠΎΠΆΠ°ΡΠΎΡΡΡΠ΅Π½ΠΈΠΈ. ΠΡΠΎΠ°Π½Π°Π»ΠΈΠ·ΠΈΡΠΎΠ²Π°Π½Ρ Π½Π΅Π΄ΠΎΡΡΠ°ΡΠΊΠΈ ΠΏΠ΅Π½Π½ΠΎΠ³ΠΎ ΠΏΠΎΠΆΠ°ΡΠΎΡΡΡΠ΅Π½ΠΈΡ, ΠΎΠ±ΡΡΠ»ΠΎΠ²Π»Π΅Π½Π½ΡΠ΅ ΡΠΈΡΡΠ΅ΠΌΠΎΠΉ Π΄ΠΎΠ·ΠΈΡΠΎΠ²Π°Π½ΠΈΡ ΠΏΠ΅Π½ΠΎΠΎΠ±ΡΠ°Π·ΠΎΠ²Π°ΡΠ΅Π»Ρ. Π Π°ΡΡΠΌΠΎΡΡΠ΅Π½Ρ Π²ΠΈΠ΄Ρ Π΄ΠΎΠ·Π°ΡΠΎΡΠΎΠ² ΠΈ ΠΏΡΠ΅Π΄Π»ΠΎΠΆΠ΅Π½Π° ΡΠ»Π΅ΠΊΡΡΠΎΠ½Π½Π°Ρ ΡΠΈΡΡΠ΅ΠΌΠ° Π΄ΠΎΠ·ΠΈΡΠΎΠ²Π°Π½ΠΈΡ "Π‘ΠΏΡΡΡ-Π‘Π"
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