Show simple item record

dc.contributor.authorIkehara, Morio
dc.date.accessioned2023-11-03T09:27:50Z
dc.date.available2023-11-03T09:27:50Z
dc.date.issued1989
dc.date.submitted2023-11-03
dc.identifier.citationAdvances in protein design, 73 - 79en_US
dc.identifier.isbn3527280243
dc.identifier.isbn0895739534
dc.identifier.issn0930-4320
dc.identifier.urihttp://hdl.handle.net/10033/623522
dc.description.abstractRibonuclease Tl (RNase T1) was found in 1975 by Sato and Egamil from Aspergillus oryzae. This enzyme catalyzes hydrolysis of single-stranded RNA at guanylic acid 3'- phosphodiester sites. By this property RNase Tl is extremely useful for elucidation of primary structure of RNA's together with pancreatic RNase. The amino acid sequence of RNase Tl has been reported in 1965 , but it was corrected later in 1985.2 This enzyme consists of 104 amino acids and two disulfide bridges between Cys 2 and 10, as well as Cys6 and 103. RNase T1 is very stable towards heating and acidic conditions and suitable for biochemical and physicochemical studies.3 Recently three dimensional structure of this enzyme was elucidated by X-ray crystallography4:5 as a complex with an inhibitor guanosine 2'-phosphate. In this paper we attempted to obtain some details of structure-function relationship of RNase Tl by means of protein engineering.en_US
dc.language.isoenen_US
dc.publisherGBF Gesellschaft für Biotechnologische Forschung mbH, Braunschweigen_US
dc.relation.ispartofseriesGBF monographs ; Volume 12en_US
dc.rightsAttribution-NonCommercial-ShareAlike 4.0 International*
dc.rights.urihttp://creativecommons.org/licenses/by-nc-sa/4.0/*
dc.titleENGINEERING OF RNASE T 1en_US
dc.typeBook chapteren_US
dc.typeconference paperen_US
dc.contributor.departmentProtein Engineering Research Institute 6-2-1 Furuedai, Suita, Osaka, Japan 565en_US
dc.identifier.journalAdvances in protein design, 1988en_US
refterms.dateFOA2023-11-03T09:27:51Z


Files in this item

Thumbnail
Name:
Ikehara73.pdf
Size:
3.726Mb
Format:
PDF
Description:
PDF

This item appears in the following Collection(s)

Show simple item record

Attribution-NonCommercial-ShareAlike 4.0 International
Except where otherwise noted, this item's license is described as Attribution-NonCommercial-ShareAlike 4.0 International