HYBRID PROTEINS
Recombinant DNA technology is employed to produce a single chain protein in which a Kringle domain and a serine protease domain of a plasminogen activator are linked to the heavy chain variable region of fibrin specific antibody. The single chain protein is associated with a complementary light chai...
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creator | JOHN SPENCER EMTAGE TIMOTHY JOHN ROY HARRIS |
description | Recombinant DNA technology is employed to produce a single chain protein in which a Kringle domain and a serine protease domain of a plasminogen activator are linked to the heavy chain variable region of fibrin specific antibody. The single chain protein is associated with a complementary light chain variable domain of an antifibrin antibody so as to form a fibrin binding site. The construct has in vitro and in vivo clot lysis activity, the activity in vivo being similar to that of tPA, while fibrin binding is enhanced relative to tPA. |
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The single chain protein is associated with a complementary light chain variable domain of an antifibrin antibody so as to form a fibrin binding site. The construct has in vitro and in vivo clot lysis activity, the activity in vivo being similar to that of tPA, while fibrin binding is enhanced relative to tPA.</description><edition>5</edition><language>eng</language><subject>BEER ; BIOCHEMISTRY ; CHEMISTRY ; COMPOSITIONS THEREOF ; CULTURE MEDIA ; ENZYMOLOGY ; HUMAN NECESSITIES ; HYGIENE ; MEDICAL OR VETERINARY SCIENCE ; METALLURGY ; MICROBIOLOGY ; MICROORGANISMS OR ENZYMES ; MUTATION OR GENETIC ENGINEERING ; ORGANIC CHEMISTRY ; PEPTIDES ; PREPARATIONS FOR MEDICAL, DENTAL, OR TOILET PURPOSES ; PROPAGATING, PRESERVING OR MAINTAINING MICROORGANISMS ; SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS ORMEDICINAL PREPARATIONS ; SPIRITS ; VINEGAR ; WINE</subject><creationdate>1990</creationdate><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://worldwide.espacenet.com/publicationDetails/biblio?FT=D&date=19900105&DB=EPODOC&CC=AU&NR=3695589A$$EHTML$$P50$$Gepo$$Hfree_for_read</linktohtml><link.rule.ids>230,308,777,882,25545,76296</link.rule.ids><linktorsrc>$$Uhttps://worldwide.espacenet.com/publicationDetails/biblio?FT=D&date=19900105&DB=EPODOC&CC=AU&NR=3695589A$$EView_record_in_European_Patent_Office$$FView_record_in_$$GEuropean_Patent_Office$$Hfree_for_read</linktorsrc></links><search><creatorcontrib>JOHN SPENCER EMTAGE</creatorcontrib><creatorcontrib>TIMOTHY JOHN ROY HARRIS</creatorcontrib><title>HYBRID PROTEINS</title><description>Recombinant DNA technology is employed to produce a single chain protein in which a Kringle domain and a serine protease domain of a plasminogen activator are linked to the heavy chain variable region of fibrin specific antibody. 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The single chain protein is associated with a complementary light chain variable domain of an antifibrin antibody so as to form a fibrin binding site. The construct has in vitro and in vivo clot lysis activity, the activity in vivo being similar to that of tPA, while fibrin binding is enhanced relative to tPA.</abstract><edition>5</edition><oa>free_for_read</oa></addata></record> |
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subjects | BEER BIOCHEMISTRY CHEMISTRY COMPOSITIONS THEREOF CULTURE MEDIA ENZYMOLOGY HUMAN NECESSITIES HYGIENE MEDICAL OR VETERINARY SCIENCE METALLURGY MICROBIOLOGY MICROORGANISMS OR ENZYMES MUTATION OR GENETIC ENGINEERING ORGANIC CHEMISTRY PEPTIDES PREPARATIONS FOR MEDICAL, DENTAL, OR TOILET PURPOSES PROPAGATING, PRESERVING OR MAINTAINING MICROORGANISMS SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS ORMEDICINAL PREPARATIONS SPIRITS VINEGAR WINE |
title | HYBRID PROTEINS |
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