Document Detail

The disintegration of surgical sutures on exposure to pancreatic juice.
MedLine Citation:
PMID:  304708     Owner:  NLM     Status:  MEDLINE    
The loop-breaking strength of various suture materials was tested over a period of 14 days during which time the sutures were incubated in vitro in saline or canine serum, bile, activated or nonactivated pancreatic juice. Under the conditions of the study, silk and nylon maintained their strength in each environment. Polyglycolic acid maintained its strength in saline, bile or serum, but gradually lost much of its strength when exposed to pancreatic juice. Catgut, both plain and chromic, disintegrated almost completely within 24-48 hours respectively when exposed to enterokinase activated pancreatic juice. Inhibition of trypsin by aprotinin (Trasylol) resulted in preservation of catgut strength but inhibition by soybean inhibitor did not. The latter findings suggest that proteolytic enzymes, other than trypsin, may be responsible for the disintegration.
K Mizuma; P C Lee; J M Howard
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Publication Detail:
Type:  Comparative Study; Journal Article; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  Annals of surgery     Volume:  186     ISSN:  0003-4932     ISO Abbreviation:  Ann. Surg.     Publication Date:  1977 Dec 
Date Detail:
Created Date:  1978-03-29     Completed Date:  1978-03-29     Revised Date:  2009-11-18    
Medline Journal Info:
Nlm Unique ID:  0372354     Medline TA:  Ann Surg     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  718-22     Citation Subset:  AIM; IM    
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MeSH Terms
Aprotinin / pharmacology
Enteropeptidase / pharmacology
Pancreatic Juice* / drug effects
Peptide Hydrolases / pharmacology
Polyglycolic Acid
Sodium Chloride / pharmacology
Tensile Strength
Trypsin Inhibitor, Kunitz Soybean / pharmacology
Reg. No./Substance:
0/Nylons; 26009-03-0/Polyglycolic Acid; 7647-14-5/Sodium Chloride; 9002-08-8/Trypsinogen; 9087-70-1/Aprotinin; 9088-41-9/Trypsin Inhibitor, Kunitz Soybean; EC 3.4.-/Peptide Hydrolases; EC

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

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