Pascal and Francis Bibliographic Databases

Help

Export

Selection :

Permanent link
http://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=4011970

Role of the S' subsites in serine protease catalysis. Active-site mapping of rat chymotrypsin, rat trypsin, α-lytic protease, and cercarial protease from Schistosoma mansoni

Author
SCHELLENBERGER, V1 ; TURCK, C. W; RUTTER, W. J1
[1] Univ. California, hormone res. inst., dep. biochemistry biophysics, San Francisco CA 94143, United States
Source

Biochemistry (Easton). 1994, Vol 33, Num 14, pp 4251-4257 ; ref : 21 ref

ISSN
0006-2960
Scientific domain
Biochemistry, molecular biology, biophysics
Publisher
American Chemical Society, Washington, DC
Publication country
United States
Document type
Article
Language
English
Keyword (fr)
Chymotrypsin Rat Relation structure fonction Schistosoma mansoni Site actif Spécificité substrat Trypsin α-Lytic endopeptidase Enzyme Helmintha Hydrolases Invertebrata Mammalia Plathelmintha Proteinases Rodentia Serine endopeptidases Trematoda Vertebrata
Keyword (en)
Chymotrypsin Rat Structure function relationship Schistosoma mansoni Active site Substrate specificity Trypsin α-Lytic endopeptidase Enzyme Helmintha Hydrolases Invertebrata Mammalia Plathelmintha Proteinases Rodentia Serine endopeptidases Trematoda Vertebrata
Keyword (es)
Chymotrypsin Rata Relación estructura función Schistosoma mansoni Lugar activo Especificidad sustrato Trypsin α-Lytic endopeptidase Enzima Helmintha Hydrolases Invertebrata Mammalia Plathelmintha Proteinases Rodentia Serine endopeptidases Trematoda Vertebrata
Classification
Pascal
002 Biological and medical sciences / 002A Fundamental and applied biological sciences. Psychology / 002A02 Analytical, structural and metabolic biochemistry / 002A02E Enzymes and enzyme inhibitors / 002A02E04 Hydrolases

Discipline
Analytical, structural and metabolic biochemistry
Origin
Inist-CNRS
Database
PASCAL
INIST identifier
4011970

Sauf mention contraire ci-dessus, le contenu de cette notice bibliographique peut être utilisé dans le cadre d’une licence CC BY 4.0 Inist-CNRS / Unless otherwise stated above, the content of this bibliographic record may be used under a CC BY 4.0 licence by Inist-CNRS / A menos que se haya señalado antes, el contenido de este registro bibliográfico puede ser utilizado al amparo de una licencia CC BY 4.0 Inist-CNRS

Access to the document

Searching the Web