Document Detail

Studies on silk secretion in the Trichoptera (F. Limmephilidae). II. Structure and amino acid composition of the silk.
MedLine Citation:
PMID:  1277288     Owner:  NLM     Status:  MEDLINE    
The ultrastructure and amino acid composition of the secreted silk of two species of trichopteran larvae, Pycnopsyche guttifer (Walk.) and Neophylax concinnus McL., were investigated. The spinnerets of these two animals were also examined by scanning electron microscopy. The silk consists of double-stranded, flat ribbons (1-4 mu wide), composed of bundles of 15-25 A filaments. There are two components of the silk: the fiber proper and a surrounding coat thought to be a silk "gum". Only the outer coat is positive to the EM PATP technique of Thiery (1967), which indicated the presence of neutral sugars. Amino acid analyses of Pycnopsyche silk show that, like other silks, two predominant amino acids are glycine and serine. Arginine, unexpectedly, is the third most abundant and there are a large number of basic and long side-chain amino acids. X-ray diffraction studies of the silk indicate that it has a less crystalline, more amorphous structure than that of other silks.
M S Engster
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Publication Detail:
Type:  Journal Article; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  Cell and tissue research     Volume:  169     ISSN:  0302-766X     ISO Abbreviation:  Cell Tissue Res.     Publication Date:  1976 Jun 
Date Detail:
Created Date:  1976-09-02     Completed Date:  1976-09-02     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  0417625     Medline TA:  Cell Tissue Res     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  77-92     Citation Subset:  IM    
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MeSH Terms
Amino Acids / analysis*
Fibroins / analysis
Microscopy, Electron
Protein Conformation
Proteins* / analysis
X-Ray Diffraction
Reg. No./Substance:
0/Amino Acids; 0/Proteins; 9007-76-5/Fibroins

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