Zobrazeno 1 - 10
of 24
pro vyhledávání: '"James E. Pitts"'
Autor:
Jon B. Cooper, P. Orprayoon, M.P. Newman, V. Dhanaraj, Tom L. Blundell, Philip Nugent, Dimitris Mantafounis, C. G. Dealwis, James E. Pitts
Publikováno v:
Scandinavian Journal of Clinical and Laboratory Investigation. 52:39-50
The specificity and pH profile of aspartic proteinases have evolved to include not only pepsin with a broad specificity and an optimal activity in acid media, but also renin, with high specificity for angiotensinogen and activity close to neutral pH.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7bb1925d2d78f47ead11c8a202b991dc
https://doi.org/10.3109/00365519209104653
https://doi.org/10.3109/00365519209104653
Publikováno v:
Pitts, J E, Quinn, D, Uusitalo, J & Penttilä, M 1991, ' Protein engineering of chymosin and expression in Trichoderma reesei ', Biochemical Society Transactions, vol. 19, no. 3, pp. 663-666 . https://doi.org/10.1042/bst0190663
Chymosin (EC 3.4.23.4) is an aspartic proteinase containing three disulphide bridges, which occurs naturally in the fourth stomach of the unweaned calf The mature enzyme initiates milk clotting by the specific cleavage of Ic-casein between the Phe105
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e6dbc6caf2df3836420a0fd8d0eb0076
https://doi.org/10.1042/bst0190663
https://doi.org/10.1042/bst0190663
Autor:
James E. Pitts, Dimitris Mantafounis
Publikováno v:
"Protein Engineering, Design and Selection". 3:605-609
The aspartic proteinase chymosin exhibits a local network of hydrogen bonds involving the active site aspartates and surrounding residues which may have an influence on the rate and optimal pH of substrate cleavage. We have introduced into chymosin B
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::10bd709a1b3529f7824696262f2c43ef
https://doi.org/10.1093/protein/3.7.605
https://doi.org/10.1093/protein/3.7.605
Autor:
James E. Pitts
Publikováno v:
Financial Review. 4:271-272
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7bbeef5989a9b8a642b60b105fe4ba83
https://doi.org/10.1111/j.1540-6288.1969.tb01736.x-i1
https://doi.org/10.1111/j.1540-6288.1969.tb01736.x-i1
Publikováno v:
Orprayoon, P, Nugent, P, Pitts, J E, Blundell, T L, Uusitalo, J M & Penttilä, M 1993, ' Prarbn engineering of a loop 155-165 in chymosin ', Protein Engineering, Design and Selection, vol. 6 . https://doi.org/10.1093/protein/6.Supplement.130-b
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3550ee7ad1086c731ed5b016f4eab076
https://doi.org/10.1093/protein/6.supplement.130-b
https://doi.org/10.1093/protein/6.supplement.130-b
Autor:
Philip Nugent, Poonsook Orprayoon, Dominic Quinn, Dimitris Mantafounis, James E. Pitts, Jaana Uusitalo, Merja Penttilä
Publikováno v:
Pitts, J E, Uusitalo, J M, Mantafounis, D, Nugent, P G, Quinn, D D, Orprayoon, P & Penttilä, M E 1993, ' Expression and characterisation of chymosin pH optima mutants produced in Trichoderma reesei ', Journal of Biotechnology, vol. 28, no. 1, pp. 69-83 . https://doi.org/10.1016/0168-1656(93)90126-8
The production of chymosin mutants designed to have altered pH optima using the cellulolytic filamentous fungus Trichoderma reesei is described. The strong promoter of the gene encoding the major cellulase, cellobiohydrolase I (CBHI) has been used fo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::00e9dbbfed1270790ae6dad68cf85721
https://cris.vtt.fi/en/publications/2fdfddc0-e709-464b-96f5-6bebb0115559
https://cris.vtt.fi/en/publications/2fdfddc0-e709-464b-96f5-6bebb0115559
Autor:
Janna Uusitalo, Raj Gill, Sean E. Lawler, Merja Penttilä, Dimitiris Mantafounis, James E. Pitts
Publikováno v:
Lawler, S E, Pitts, J E, Mantafounis, D, Gill, R, Uusitalo, J & Penttila, M 1991, ' Secretion of a chymosin-insulin fusion in Trichoderma reesei ', Biochemical Society Transactions, vol. 19, no. 3 . https://doi.org/10.1042/bst019248s
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::13f613dc18bc237d6a95bb81e3fc51de
https://cris.vtt.fi/en/publications/9682fcf6-8bdb-4d58-b8ce-60d3631cd4e4
https://cris.vtt.fi/en/publications/9682fcf6-8bdb-4d58-b8ce-60d3631cd4e4
Autor:
Dimitris Mantafounis, Tom L. Blundell, Sean E. Lawler, Merja Penttilä, Philip Nugent, Poonsook Orprayoon, James E. Pitts, Janna Uusitalo
Publikováno v:
Orprayoon, P, Pitts, J E, Nugent, P, Mantafounis, D, Lawler, S E, Blundell, T L, Uusitalo, J & Penttilä, M 1991, ' Protein engineering of the surface loops of chymosin ', Biochemical Society Transactions, vol. 19, no. 3 . https://doi.org/10.1042/bst019265s
Scopus-Elsevier
Scopus-Elsevier
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2f3aeb84b911d93f364ad37d6117a386
https://pubmed.ncbi.nlm.nih.gov/1783113
https://pubmed.ncbi.nlm.nih.gov/1783113
Autor:
James E. Pitts, Dimitris Mantafounis
Publikováno v:
Biochemical Society transactions. 19(3)
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b50e4745d41afa47f06ff6097f7378ea
https://pubmed.ncbi.nlm.nih.gov/1783114
https://pubmed.ncbi.nlm.nih.gov/1783114
Autor:
S.Edward Lee, Peter John Whittle, Stephen Hawrylik, Andrew M. Hemmings, James Merson, James E. Pitts, John P. Overington, Kathryn Shield, Andrew F. Wilderspin, S. P. Wood, Kieran Francis Geoghegan, Laurence H. Pearl, R. Lapatto, Peter M. Hobart, Tom L. Blundell, Dennis Edward Danley, Duncan J. H. Gaskin, Zhang-Yang Zhu
Publikováno v:
Retroviral Proteases ISBN: 9780333536124
HIV-1 proteinase processes its virally encoded polyproteins into mature structural proteins and enzymes that are essential for viral propagation. As a consequence the proteinase is an attractive target for prospective antiviral agents for the treatme
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::344cecd549e9dbb42146cbca1fdbf640
https://doi.org/10.1007/978-1-349-11907-3_10
https://doi.org/10.1007/978-1-349-11907-3_10