Any feedback?
Please rate this page
(all_enzymes.php)
(0/150)

BRENDA support

3.4.21.68: t-Plasminogen activator

This is an abbreviated version!
For detailed information about t-Plasminogen activator, go to the full flat file.

Word Map on EC 3.4.21.68

Reaction

Specific cleavage of Arg-/-Val bond in plasminogen to form plasmin =

Synonyms

Alteplase, BAT-PA, desmoteplase, DSPA beta, DSPA gamma, EC 3.4.21.31, EC 3.4.99.26, human tissue-type plasminogen activator, IV t-PA, IV tissue plasminogen activator, More, plasminogen activator, Plasminogen activator, tissue-type, PLAT, r-tPA, recombinant tissue plasminogen activator, Reteplase, rt-PA, rtPA, sc-tPA, sctPA, single chain enzyme tPA, t-PA, t-PA protein, t-plasminogen activator, tc-tPA, tctPA, Tissue plasminogen activator, tissue type plasminogen activator, tissue-plasminogen activator, Tissue-type plasminogen activator, tissue-type plasmiongen activator, tPA, two chain tPA

ECTree

     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.21 Serine endopeptidases
                3.4.21.68 t-Plasminogen activator

Purification

Purification on EC 3.4.21.68 - t-Plasminogen activator

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
glycosylation variant of human tPA
-
mutant N117Q/N184Q
-
one-step purification using affinity chromatography with a special monoclonal antibody
-
recombinant active full-length and active truncated 650 bp enzymes from Nicotiana tabacum by lysine affinity chromatography and gel filtration
-
recombinant chimeric tissue plasminogen activator mutant from Nicotiana tabacum hairy roots by lysine affinity chromatography. In addition, specific aptamers are designed using SELEX method. Multi wall carbon nanotubes are functionalized with selected aptamers, Chi-tPA1-5, packed in a column, and used for purification. The selected aptamer Chi-tPA1, having KD values of 0.320 nM and IC50 of 28.9 nM, possesses good affinity to tPA, and the chimeric mutant tPA is properly purified by aptamer-chromatography. Development of aptamer-based affinity purification method, overview
recombinant enzyme
-
recombinant His-tagged kringle 2 plus serine protease domains, K2S, of human tissue plasminogen activator from Escherichia coli by nickel affinity chromatography after cleavage with factor Xa
-
recombinant His-tagged soluble full-length enzyme tPA from Escherichia coli by nickel affinity chromatography, the His-tag is cleaved off by PreScission Protease (PSP), leaving only two additional residues (Gly and Pro) at the N-terminus, followed by gel filtration
recombinant His-tagged truncated enzyme from Leishmania tarentolae by nickel affinity chromatography
-
recombinant His6-tagged truncated enzyme form K2S from Nicotiana tabacum chloroplasts by nickel affinity chromatography and dialysis, the His-tag is cleaved off by protease factor Xa
recombinant wild-type and mutant isolated serine protease domain (residues 276-527)of enzyme tPA from Pichia pastoris strain X-33 by cation exchange chromatography and gel filtration
using a lysine-sepharose column.Two chain tPA is generated from wild-type tPA by incubation with plasmin-sepharose
-
wild type and recombinant enzyme
-