Related Experiment Video
Updated: May 27, 2026
10:27
Recognition of Epidermal Transglutaminase by IgA and Tissue Transglutaminase 2 Antibodies in a Rare Case of Rhesus Dermatitis
Published on: December 15, 2011
Residual transglutaminase in collagen - effects, detection, quantification, and removal
1Department of Pharmacy, Pharmaceutical Technology and Biopharmaceutics, Ludwig-Maximilians-University, Munich, Germany. winfried.schloegl@gmx.de
Summary
A new enzyme-linked immunosorbent assay (ELISA) quantifies microbial transglutaminase (mTG). Most mTG binds non-covalently to modified collagen, but dialysis effectively removes it, unlike washing or chemical treatments.
Area of Science:
- Biochemistry
- Enzymology
- Materials Science
Background:
- Microbial transglutaminase (mTG) is crucial for modifying collagen.
- Quantification of mTG residuals in modified collagen is challenging.
- Understanding mTG binding is vital for biomaterial applications.
Purpose of the Study:
- Develop a reliable quantification method for mTG.
- Investigate mTG residuals in mTG-modified porcine collagen type I.
- Evaluate methods for mTG removal from modified collagen.
Main Methods:
- Developed an enzyme-linked immunosorbent assay (ELISA) for mTG quantification.
- Analyzed mTG residuals in collagen using ELISA and Western blot.
- Assessed mTG removal via washing, dialysis, and chemical treatments.
Main Results:
- ELISA successfully quantified mTG from Streptomyces mobaraensis.
- Up to 40% of mTG remained non-covalently bound to modified collagen.
- Acidic/alkaline dialysis completely removed mTG; washing and chemical treatments were less effective.
Conclusions:
- A validated ELISA method for mTG quantification is now available.
- Non-covalent binding of mTG to collagen necessitates effective removal strategies.
- Dialysis is a highly effective method for removing residual mTG from collagen materials.
