Document Detail


Structural studies on des-pentapeptide (B26-30)-insulin. I. The preparation and properties of des-pentapeptide-insulin.
MedLine Citation:
PMID:  788152     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
It has been suggested in our previous reports that the B-chain C-terminal peptide sequence of the insulin molecule plays an important role in the primary biological activity of this hormone. It is interesting, therefore, to study the structure-function relationship of a series of related insulin analogues. An improved method has been used in this paper for the preparation of des-pentapeptide (B26-30)-insulin (DPI) suitable for the growth of single crystals. These crystals possess 88% of the receptor binding activity of insulin and exhibit hormonal activity of 20 I.U. per milligramme in the mouse convulsion test. In the presence of zinc ions, DPI cross-reacts immunologically with insulin antibody.
Authors:
-
Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  Scientia Sinica     Volume:  19     ISSN:  0250-7870     ISO Abbreviation:  Sci. Sin.     Publication Date:    1976 May-Jun
Date Detail:
Created Date:  1976-11-21     Completed Date:  1976-11-21     Revised Date:  2003-11-14    
Medline Journal Info:
Nlm Unique ID:  8209876     Medline TA:  Sci Sin     Country:  CHINA    
Other Details:
Languages:  eng     Pagination:  351-7     Citation Subset:  IM    
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MeSH Terms
Descriptor/Qualifier:
Amino Acids / analysis
Animals
Insulin*
Mice
Pepsin A
Peptide Fragments* / analysis
Chemical
Reg. No./Substance:
0/Amino Acids; 0/Peptide Fragments; 11061-68-0/Insulin; EC 3.4.23.1/Pepsin A

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


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