Document Detail


Amino acid sequence and S-S bonds of Penicillium brevicompactum guanyl-specific ribonuclease.
MedLine Citation:
PMID:  6437869     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The primary structure of Penicillium brevicompactum guanyl-specific RNase was determined. The enzyme consists of 102 amino acid residues, Mr 10801. The 4 cysteine residues of the RNase are linked in pairs by disulfide bonds: Cys2-Cys10, Cys6-Cys101. P. brevicompactum RNase structure is similar to RNase T1; the degree of homology is 66%.
Authors:
S V Shlyapnikov; V A Kulikov; G I Yakovlev
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Publication Detail:
Type:  Comparative Study; Journal Article    
Journal Detail:
Title:  FEBS letters     Volume:  177     ISSN:  0014-5793     ISO Abbreviation:  FEBS Lett.     Publication Date:  1984 Nov 
Date Detail:
Created Date:  1985-01-09     Completed Date:  1985-01-09     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  0155157     Medline TA:  FEBS Lett     Country:  NETHERLANDS    
Other Details:
Languages:  eng     Pagination:  246-8     Citation Subset:  IM    
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MeSH Terms
Descriptor/Qualifier:
Amino Acid Sequence
Disulfides / analysis
Endoribonucleases*
Penicillium / enzymology*
Peptide Fragments / analysis
Ribonuclease T1*
Chemical
Reg. No./Substance:
0/Disulfides; 0/Peptide Fragments; EC 3.1.-/Endoribonucleases; EC 3.1.27.3/Ribonuclease T1

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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