| Synthesis of a trihexacontapeptide corresponding to the sequence 8-70 of eglin c and studies on the relationship between the structure and the inhibitory activity against human leukocyte elastase, cathepsin G and alpha-chymotrypsin. | |
| | |
MedLine Citation:
|
PMID: 2226822 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
|
A trihexacontapeptide corresponding to the sequence 8-70 of eglin c and its related peptides were synthesized by the conventional solution method and their inhibitory activity against human leukocyte elastase, cathepsin G and alpha-chymotrypsin was examined. Although synthetic eglin c (41-49) inhibited cathepsin G and alpha-chymotrypsin (Ki = 4.0 x 10(-5) M and 2.0 x 10(-5) M, respectively) but not leukocyte elastase, the synthetic trihexacontapeptide potently inhibited cathepsin G, alpha-chymotrypsin and leukocyte elastase (Ki = 1.8 x 10(-9) M, 1.4 x 10(-9) M and 2.2 x 10(-9) M, respectively). The relationship between the structure of eglin c and the inhibitory activity against the above enzymes is also described. |
| | |
Authors:
|
Y Okada; S Tsuboi; Y Tsuda; Y Nagamatsu; J Yamamoto |
Publication Detail:
|
Type: Comparative Study; Journal Article; Research Support, Non-U.S. Gov't |
Journal Detail:
|
Title: FEBS letters Volume: 272 ISSN: 0014-5793 ISO Abbreviation: FEBS Lett. Publication Date: 1990 Oct |
Date Detail:
|
Created Date: 1990-12-13 Completed Date: 1990-12-13 Revised Date: 2009-11-19 |
Medline Journal Info:
|
Nlm Unique ID: 0155157 Medline TA: FEBS Lett Country: NETHERLANDS |
Other Details:
|
Languages: eng Pagination: 113-6 Citation Subset: IM |
Affiliation:
|
Faculty of Pharmaceutical Sciences, Kobe-Gakuin University, Japan. |
Export Citation:
|
APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
|
Amino Acid Sequence Cathepsin G Cathepsins / antagonists & inhibitors* Chymotrypsin / antagonists & inhibitors* Electrochemistry Humans Hydrogen Bonding Leukocyte Elastase Molecular Sequence Data Pancreatic Elastase / antagonists & inhibitors* Peptide Fragments / chemical synthesis*, chemistry, pharmacology Proteins Serine Endopeptidases Serine Proteinase Inhibitors / chemistry* Serpins* Structure-Activity Relationship |
| Chemical | |
Reg. No./Substance:
|
0/Peptide Fragments; 0/Proteins; 0/Serine Proteinase Inhibitors; 0/Serpins; 0/eglin proteinase inhibitors; EC 3.4.-/Cathepsins; EC 3.4.21.-/Serine Endopeptidases; EC 3.4.21.1/Chymotrypsin; EC 3.4.21.20/CTSG protein, human; EC 3.4.21.20/Cathepsin G; EC 3.4.21.36/Pancreatic Elastase; EC 3.4.21.37/Leukocyte Elastase |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
Previous Document: Conformational changes in human fibrinogen after in vitro phosphorylation and their relation to fibr...
Next Document: Luminol enhanced chemiluminescence of the perfused rat heart during ischemia and reperfusion.